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More than half of the global population is unable to consume dairy products due to lactose intolerance (hypolactasia). Current enzyme replacement therapy methods are insufficiently effective as a therapeutic approach to treating lactose intolerance. The encapsulation of β-galactosidase in polyelectrolyte microcapsules by using the layer-by-layer method could be a possible solution to this problem. In this study, adsorption and co-precipitation methods were employed for encapsulating β-galactosidase in polyelectrolyte microcapsules composed of (polyallylamine /polystyrene sulphonate)₃. As a result, the co-precipitation method was chosen for β-galactosidase encapsulation. The adsorption method permits to encapsulate six times less enzyme compared with the co-precipitation method; the β-galactosidase encapsulated via the co-precipitation method released no more than 20% of the initially encapsulated enzyme in pH 2 or 1 M NaCl solutions. In contrast, when using the sorption method, about 100% of the initially encapsulated enzyme was released from the microcapsules under the conditions described above. The co-precipitation method effectively prevents the complete loss of enzyme activity after 2 h of incubation in a solution with pH 2 while also alleviating the adverse effects of ionic strength. Consequently, the encapsulated form of β-galactosidase shows promise as a potential therapeutic agent for enzyme replacement therapy in the treatment of hypolactasia. [ABSTRACT FROM AUTHOR]

The article presents the review and synthesis of mo­dern data of scientific publications from the Scopus, Web of Science databases, and the register of professional scientific publications of Ukraine on the causes, consequences, and methods of correcting secondary lactase deficiency in children. The features of secondary lactase deficiency in antibiotic therapy and other pathological changes in the gastrointestinal tract that develop with the use of antibacterial drugs are described. The authors present their own data on the treatment of secondary lactase deficiency caused by antibiotic therapy in school-age children. It has been found that the use of the lactase enzyme in children with secon­dary lactase deficiency, which has developed on the background of antibiotic therapy, leads to positive dynamics of clinical manifestations already on the third day of taking the drug, and it is a more effective method of correcting these symptoms compared to only dietary recommendations and limited consumption of lactose products. The criteria proposed for prescribing a hydrogen breath test to diagnose secondary lactase deficiency developed on the background of antibiotics are as follows: the presence of clinical manifestations (diarrhea, abdominal pain, excessive gas, bloating, nausea, vomiting) that occurred during antibiotic therapy and are aggravated by the use of lactose-containing products; repeated courses of antibacterial drugs (every 3–4 months) according to the anamnesis; changes in the results of the coprogram (yellow, mushy, foamy feces with an acidic odor, the presence of mucus, fecal pH less than 5.5, a small amount of iodophilic flora); no signs of inflammatory bowel disease according to the results of the coprogram (blood, leukocytes); negative results of rapid tests for the detection of Clostridium difficile toxins A and B in the feces. The use of these criteria to diagnose secondary lactase deficiency associated with antibiotics will improve the frequency of its detection and the reasonable prescription of lactase drugs to reduce the severity of clinical manifestations of lactase deficiency and restore the functional state of the gastrointestinal tract more quickly.

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Bacillus licheniformis strain DSM 34099 by Kerry Group Services International, Ltd. (KGSI). The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. The production strain met the requirements for the qualified presumption of safety (QPS) approach. The food enzyme is intended to be used in two food manufacturing processes. Dietary exposure was estimated to be up to 7.263 mg total organic solids/kg body weight per day in European populations. Given the QPS status of the production strain and the absence of concerns resulting from the food enzyme manufacturing process, toxicity tests, other than an assessment of allergenicity, were considered unnecessary by the Panel. A search for the identity of the amino acid sequence of the food enzyme to known allergens was made and one match with a food allergen from kiwi fruit was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme, particularly in individuals sensitised to kiwi fruit, cannot be excluded. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use. [ABSTRACT FROM AUTHOR]

Objective: In this retrospective study, we assessed the efficacy of oral lactase in infants with lactose intolerance in terms of sex, birth weight, and interference by other medications. Methods: The study was conducted on patients aged 0–6 months who had been diagnosed with lactose intolerance on admission to the Department of Social Pediatrics at Dokuz Eylul University. Demographic data, the onset of symptoms, and medications used were recorded. Results: We found that 86.7% of the infants responded to lactase, with no significant differences based on sex, birth weight, or age at symptom presentation. We observed, however, that the efficacy of treatment did improve over time, thereby deriving benefits from intestinal development and adaptation. Interestingly, the response to lactase was reduced in infants receiving concomitant simethicone for colic symptoms, suggesting a potential drug interaction, while probiotics had no impact on treatment outcomes. Conclusions: We advise against using additional medications with oral lactase, pointing out a possible interaction with simethicone that might decrease the effectiveness of treatment. [ABSTRACT FROM AUTHOR]

Evidence for a reduction in stature between Mesolithic foragers and Neolithic farmers has been interpreted as reflective of declines in health, however, our current understanding of this trend fails to account for the complexity of cultural and dietary transitions or the possible causes of phenotypic change. The agricultural transition was extended in primary centers of domestication and abrupt in regions characterized by demic diffusion. In regions such as Northern Europe where foreign domesticates were difficult to establish, there is strong evidence for natural selection for lactase persistence in relation to dairying. We employ broad-scale analyses of diachronic variation in stature and body mass in the Levant, Europe, the Nile Valley, South Asia, and China, to test three hypotheses about the timing of subsistence shifts and human body size, that: 1) the adoption of agriculture led to a decrease in stature, 2) there were different trajectories in regions of in situ domestication or cultural diffusion of agriculture; and 3) increases in stature and body mass are observed in regions with evidence for selection for lactase persistence. Our results demonstrate that 1) decreases in stature preceded the origins of agriculture in some regions; 2) the Levant and China, regions of in situ domestication of species and an extended period of mixed foraging and agricultural subsistence, had stable stature and body mass over time; and 3) stature and body mass increases in Central and Northern Europe coincide with the timing of selective sweeps for lactase persistence, providing support for the "Lactase Growth Hypothesis."

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Bacillus licheniformis strain DSM 34099 by Kerry Group Services International, Ltd. (KGSI). The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. The production strain met the requirements for the qualified presumption of safety (QPS) approach. The food enzyme is intended to be used in two food manufacturing processes. Dietary exposure was estimated to be up to 7.263 mg total organic solids/kg body weight per day in European populations. Given the QPS status of the production strain and the absence of concerns resulting from the food enzyme manufacturing process, toxicity tests, other than an assessment of allergenicity, were considered unnecessary by the Panel. A search for the identity of the amino acid sequence of the food enzyme to known allergens was made and one match with a food allergen from kiwi fruit was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme, particularly in individuals sensitised to kiwi fruit, cannot be excluded. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.

Lactose intolerance is a gastrointestinal condition in which lactase enzyme is unable to hydrolyze lactose into glucose and galactose. It is manifested by diarrhea, flatulence, cramping, borborygmi, and abdominal discomfort following lactose ingestion. Adverse effects also include bone decay, fractures, and osteoporosis. The development of condition due to genetic, or environmental factors could be diagnosed by hydrogen breath test, lactose tolerance test, intestinal biopsies, and genetic tests. Frequently employed traditional therapeutic approaches include lactase supplements, lactose free products, non-dairy alternatives, and probiotics. With increase in demand of more efficient diagnostic and therapeutic criteria for lactose intolerance advanced nanotechnology-based diagnostic, therapeutic, and managing approaches have been developed. Development of nanobiosensors, nano-detectors, and lactose trackers for efficient diagnosis, enzyme nanoimmobilization strategies including adsorption, encapsulation, and entrapment, delivery strategies for lactase enzyme, probiotics, and production of lactose free products had been successfully investigated under the wide umbrella of nanotechnology. This review focuses on the developments being done by the amalgamation of conventional diagnostic and therapeutic approaches. It covers the novel nanotechnological applications discovered over the years to develop the most effective diagnostic, and therapeutic procedures to ameliorate the symptoms in lactose intolerant individuals.

ObjectiveTryptophan can be catabolised to various metabolites through host kynurenine and microbial indole pathways. We aimed to examine relationships of host and microbial tryptophan metabolites with incident type 2 diabetes (T2D), host genetics, diet and gut microbiota.MethodWe analysed associations between circulating levels of 11 tryptophan metabolites and incident T2D in 9180 participants of diverse racial/ethnic backgrounds from five cohorts. We examined host genome-wide variants, dietary intake and gut microbiome associated with these metabolites.ResultsTryptophan, four kynurenine-pathway metabolites (kynurenine, kynurenate, xanthurenate and quinolinate) and indolelactate were positively associated with T2D risk, while indolepropionate was inversely associated with T2D risk. We identified multiple host genetic variants, dietary factors, gut bacteria and their potential interplay associated with these T2D-relaetd metabolites. Intakes of fibre-rich foods, but not protein/tryptophan-rich foods, were the dietary factors most strongly associated with tryptophan metabolites. The fibre-indolepropionate association was partially explained by indolepropionate-associated gut bacteria, mostly fibre-using Firmicutes. We identified a novel association between a host functional LCT variant (determining lactase persistence) and serum indolepropionate, which might be related to a host gene-diet interaction on gut Bifidobacterium, a probiotic bacterium significantly associated with indolepropionate independent of other fibre-related bacteria. Higher milk intake was associated with higher levels of gut Bifidobacterium and serum indolepropionate only among genetically lactase non-persistent individuals.ConclusionHigher milk intake among lactase non-persistent individuals, and higher fibre intake were associated with a favourable profile of circulating tryptophan metabolites for T2D, potentially through the host-microbial cross-talk shifting tryptophan metabolism toward gut microbial indolepropionate production.

Due to its very early introduction, cow's milk is one of the first foods that can cause adverse reactions in human beings. Lactose intolerance (LI) and cow's milk allergy (CMA) are the most common adverse reactions to cow's milk. While LI is due to insufficient small intestinal lactase activity and/or a large quantity of ingested lactose, CMA is an aberrant immune reaction to cow's milk proteins, particularly casein or β-lactoglobulin. However, the clinical manifestations of LI and CMA, particularly their gastrointestinal signs and symptoms, are very similar, which might lead to misdiagnosis or delayed diagnosis as well as nutritional risks due to inappropriate dietary interventions or unnecessary dietary restriction. Formula-fed infants with LI should be treated with formula with reduced or no lactose, while those with CMA should be treated with formula containing extensive hydrolyzed cow's milk protein or amino acids. This review is therefore written to assist clinicians to better understand the pathophysiologies of LI and CMA as well as to recognize the similarities and differences between clinical manifestations of LI and CMA. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Papiliotrema terrestris strain AE‐BLC by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in the production of galacto‐oligosaccharides (GOS) from lactose. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 0.441 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1800 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 4082. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

Galacto-oligosaccharides (GOS) are products of transgalactosylation reaction of β-galactosidase when lactose is used as the substrate. These carbohydrates are considered prebiotics which stimulate beneficial effects to human health. In the present work, Saphera, a commercial preparation of β-galactosidase from Bifidobacterium bifidum, was biochemically characterised for production of GOS. Using o-nitrophenyl-β-Dgalactopyranoside (oNPG) as the substrate, optimal activity for the enzyme was found to be at pH 6.0 and at 45°C. Ten (10) mM each of either Na+ or K+ enhanced enzyme activity by 10%, while Cu2+, Zn2+, Fe2+, and EDTA showed inhibitory effect on the enzyme activity. When incubated in 50 mM sodium phosphate and pH 6.5, the enzyme was found to have half-life time of 136 ± 6 and 2.1 ± 0.2 h at 30 and 50°C, respectively. The hydrolysis activity of the enzyme predominated when the initial lactose concentration used was 5% (w/v). When initial lactose concentration was increased to 20% (w/v), maximum GOS yield obtained was 10% (w/w) achieved at 86% lactose conversion. Analysis using high performance anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD) revealed that the major oligosaccharides produced by the enzyme were 3'-galactosylglucose, 3'-galactosyllactose, 3'-galactobiose, and allolactose, thus showing that this enzyme would prefer to form β-(1→3)- and β-(1→6)-linked GOS. Despite its predominantly hydrolytic activity, Saphera synthesised prebiotic GOS which could be interesting to dairy industry. [ABSTRACT FROM AUTHOR]

Human genetic variation affects the gut microbiota through a complex combination of environmental and host factors. Here we characterize genetic variations associated with microbial abundances in a single large-scale population-based cohort of 5,959 genotyped individuals with matched gut microbial metagenomes, and dietary and health records (prevalent and follow-up). We identified 567 independent SNP-taxon associations. Variants at the LCT locus associated with Bifidobacterium and other taxa, but they differed according to dairy intake. Furthermore, levels of Faecalicatena lactaris associated with ABO, and suggested preferential utilization of secreted blood antigens as energy source in the gut. Enterococcus faecalis levels associated with variants in the MED13L locus, which has been linked to colorectal cancer. Mendelian randomization analysis indicated a potential causal effect of Morganella on major depressive disorder, consistent with observational incident disease analysis. Overall, we identify and characterize the intricate nature of host-microbiota interactions and their association with disease.

Objective: In this retrospective study, we assessed the efficacy of oral lactase in infants with lactose intolerance in terms of sex, birth weight, and interference by other medications. Methods: The study was conducted on patients aged 0–6 months who had been diagnosed with lactose intolerance on admission to the Department of Social Pediatrics at Dokuz Eylul University. Demographic data, the onset of symptoms, and medications used were recorded. Results: We found that 86.7% of the infants responded to lactase, with no significant differences based on sex, birth weight, or age at symptom presentation. We observed, however, that the efficacy of treatment did improve over time, thereby deriving benefits from intestinal development and adaptation. Interestingly, the response to lactase was reduced in infants receiving concomitant simethicone for colic symptoms, suggesting a potential drug interaction, while probiotics had no impact on treatment outcomes. Conclusions: We advise against using additional medications with oral lactase, pointing out a possible interaction with simethicone that might decrease the effectiveness of treatment.

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Papiliotrema terrestris strain AE‐BLC by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in the production of galacto‐oligosaccharides (GOS) from lactose. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 0.441 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1800 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 4082. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Introduction: Lactose intolerance is a widespread problem that affects people of many different races all over the world. The following pharmacological supplements can improve the lives of those who suffer from this issue. Methods: This work focused on lactase producer isolation and statistical design (Plackett-Burman, and BOX-Behnken) to maximize the effectiveness of environmental factors. A lactase-producing bacterium was chosen from a discovery of 100 strains in soil that had previously been polluted with dairy products. Plackett-Burman investigated fifteen variables. Results: The most critical variables that lead to increased lactase synthesis are glucose, peptone, and magnesium sulfate (MgSO4). The ideal process conditions for the creation of lactase yield among the stated variables were then determined using a BOX-Benken design. To establish a polynomial quadratic relationship between the three variables and lactase activity, the Box-Behnken design level was used. The EXCEL-solver nonlinear optimization technique was used to predict the best form for lactase production. The ideal temperature and pH levels have been determined, both before and after the lactase purification process, to achieve the highest performance of isolated lactase. Conclusion: According to this study, Bacillus licheniformis is a perfect supply of the lactase enzyme (ß -Galactosidase), It can be used as a product to assist people who have health issues due to lactose intolerance. [ABSTRACT FROM AUTHOR]

Lactase is a member of the β-galactosidase family of enzymes that can hydrolyze lactose into galactose and glucose. However, extracellular lactase production was still restricted to the process of cell lysis. In this study, lactase-producing Kluyveromyces lactis JNXR-2101 was obtained using a rapid and sensitive method based on the fluorescent substrate 4-methylumbelliferyl-β-d-galactopyranoside. The purified enzyme was identified as a neutral lactase with an optimum pH of 9. To facilitate extracellular production of lactase, a putative mannoprotein KLLA0_E01057g of K. lactis was knocked out. It could effectively promote cell wall degradation and lactase production after lyticase treatment, which showed potential on other extracellular enzyme preparation. After optimizing the fermentation conditions, the lactase yield from mannoprotein-deficient K. lactis JNXR-2101ΔE01057g reached 159.62 U/mL in a 5-L fed-batch bioreactor.

To study the effect of host genetics on gut microbiome composition, the MiBioGen consortium curated and analyzed genome-wide genotypes and 16S fecal microbiome data from 18,340 individuals (24 cohorts). Microbial composition showed high variability across cohorts: only 9 of 410 genera were detected in more than 95% of samples. A genome-wide association study of host genetic variation regarding microbial taxa identified 31 loci affecting the microbiome at a genome-wide significant (P

IntroductionLactose intolerance is a widespread problem that affects people of many different races all over the world. The following pharmacological supplements can improve the lives of those who suffer from this issue.MethodsThis work focused on lactase producer isolation and statistical design (Plackett–Burman, and BOX–Behnken) to maximize the effectiveness of environmental factors. A lactase-producing bacterium was chosen from a discovery of 100 strains in soil that had previously been polluted with dairy products. Plackett-Burman investigated fifteen variables.ResultsThe most critical variables that lead to increased lactase synthesis are glucose, peptone, and magnesium sulfate (MgSO4). The ideal process conditions for the creation of lactase yield among the stated variables were then determined using a BOX-Benken design. To establish a polynomial quadratic relationship between the three variables and lactase activity, the Box–Behnken design level was used. The EXCEL-solver nonlinear optimization technique was used to predict the best form for lactase production. The ideal temperature and pH levels have been determined, both before and after the lactase purification process, to achieve the highest performance of isolated lactase.ConclusionAccording to this study, Bacillus licheniformis is a perfect supply of the lactase enzyme (β -Galactosidase), It can be used as a product to assist people who have health issues due to lactose intolerance.

With increasing health awareness worldwide, lactose intolerance has become a major concern of consumers, creating new market opportunities for low-lactose/lactose-free dairy foods. In recent years, through innovating processes and technologies, dairy manufacturers have significantly improved the variety, and functional and sensory qualities of low-lactose and lactose-free dairy products. Based on this, this paper first covers the pathology and epidemiology of lactose intolerance and market trends. Then, we focus on current advantages and disadvantages of different lactose hydrolysis technologies and improvements in these technologies to enhance nutritional value, and functional, sensory, and quality properties of lactose-free dairy products. We found that more and more cutting-edge technologies are being applied to the production of lactose-free dairy products, and that these technologies greatly improve the quality and production efficiency of lactose-free dairy products. Hopefully, our review can provide a theoretical basis for the marketing expansion and consumption guidance for low-lactose/lactose-free dairy products. [ABSTRACT FROM AUTHOR]

The maritime expansion of Scandinavian populations during the Viking Age (about AD 750-1050) was a far-flung transformation in world history1,2. Here we sequenced the genomes of 442 humans from archaeological sites across Europe and Greenland (to a median depth of about 1×) to understand the global influence of this expansion. We find the Viking period involved gene flow into Scandinavia from the south and east. We observe genetic structure within Scandinavia, with diversity hotspots in the south and restricted gene flow within Scandinavia. We find evidence for a major influx of Danish ancestry into England; a Swedish influx into the Baltic; and Norwegian influx into Ireland, Iceland and Greenland. Additionally, we see substantial ancestry from elsewhere in Europe entering Scandinavia during the Viking Age. Our ancient DNA analysis also revealed that a Viking expedition included close family members. By comparing with modern populations, we find that pigmentation-associated loci have undergone strong population differentiation during the past millennium, and trace positively selected loci-including the lactase-persistence allele of LCT and alleles of ANKA that are associated with the immune response-in detail. We conclude that the Viking diaspora was characterized by substantial transregional engagement: distinct populations influenced the genomic makeup of different regions of Europe, and Scandinavia experienced increased contact with the rest of the continent.

Milk is a fundamental component of the human diet. Approximately 60% of the adult population worldwide has lactose intolerance. Lactose intolerance occurs due to the inability of the small intestine to produce enough enzymes to digest lactose. The purpose of the research is to study the prospects for the production of lactose-free products. Statistical and research data have been analyzed by the method of generalization of scientific publications of Russian and foreign authors on the study of lactose structure and properties, lactose intolerance syndrome, methods of β-galactosidase isolation and the use of lactose-free products. It has been stated in the research that the symptoms of lactose intolerance include abdominal pain, diarrhea, flatulence. Also, people with lactose intolerance have an increased risk of developing various extra-intestinal diseases, including cancer. Lactose intolerance makes people consume fewer dairy products, which can lead to a deficiency of calcium and other important nutrients. The article describes in detail the causes of lactose intolerance and its role in the human body. It has been shown that the development of lactose-free functional food products that meet the needs of consumers is one of the food industry priorities today. It has been established that the lactose-free dairy products market is the fastest growing segment of the dairy industry. The advantages of including lactose-free dairy products in the human diet have also been investigated, and the prospects for their production described. It has been shown that lactose-free dairy products are able to provide a person unable to digest lactose with the necessary nutrients present in conventional dairy products, such as calcium and vitamins.

Currently, there is an increase in the incidence of inflammatory bowel disease in children, including Crohn’s disease. Detection of typical endoscopic signs is the gold endoscopic standard for this disease diagnosis. When such endoscopic picture is accompanied by chronic diarrhea, abdominal pain, weight loss, and laboratory changes in the form of increased levels of faecal calprotectin and C-reactive protein, the diagnosis of Crohn’s disease becomes apparent and the diagnostic search is stopped. But there are other diseases, including of infectious type, that may have similar clinical, laboratory and endoscopic symptoms, which should be included in the scope of diagnostic search. Aim. To acquaint physicians with the features of diagnosis and monitoring of a patient with Yersinia infection on the background of lactase deficiency, clinically reminiscent of Crohn’s disease. Clinical case. A boy, 14 years old, complained of abdominal pain, recurrent diarrhea, weakness, lack of weight gain. A mother considered the child sick for 9 months, when periodic abdominal pain, diarrhea up to 10–12 times a day, sometimes nausea and vomiting occurred. Over time, episodes of diarrhea became more frequent, mainly after drinking milk. Four months after the disease onset, the child lost appetite, developed weakness, abdominal pain, recurrent diarrhea, no weight gain with increasing body length. Eight months after presenting complaints, the child was admitted to a hospital with acute disease manifestations (fever, abdominal pain, vomiting, diarrhea for 10 days). The boy was examined by a surgeon and a pediatric gastroenterologist. During colonoscopy, terminal ileitis was detected. The boy received non-specific treatment (mesalazine 3 g/day, etc.), there was a rapid improvement: abdominal pain disappeared, asthenic syndrome regressed, diarrhea reduced. Although amnestic, clinical, laboratory and instrumental data were very characteristic of Crohn’s disease, the diagnosis was questionable due to the lack of inflammatory changes in the general blood test and the fact that spontaneous remission of such severe exacerbation, for which mesalazine was usually ineffective. It was necessary to exclude other causes of inflammation of the small intestine (intestinal infections, tuberculosis). RNGA with pseudotuberculosis diagnosticum gave a positive result (intestinal yersiniosis diagnosticum O3). Conclusions. In children with suspected inflammatory bowel disease, intestinal infections, namely yersinia infection, should be ruled out as the cause of symptoms. Even with clear manifestations of terminal ileitis, which is characteristic of Crohn’s disease, the results of intestinal endoscopy may be relatively nonspecific, so the disease history, a correspondence with laboratory results, serological markers of some infectious diseases should also be taken into account in the diagnostic process for the ileitis etiology.

Lactase non-persistence (LNP), one of the causes of lactose intolerance, is related to lactase gene associated single nucleotide polymorphisms (SNPs). Since the frequency of LNP varies by ethnic group and country, the research to reveal the presence or absence of LNP for specific people has been conducted worldwide. However, in East Asia, the study of lactase gene associated SNPs have not been sufficiently examined so far using ancient human specimens from archaeological sites. In our study of Joseon period human remains (n=14), we successfully revealed genetic information of lactase gene associated SNPs (rs1679771596, rs41525747, rs4988236, rs4988235, rs41380347, rs869051967, rs145946881 and rs182549), further confirming that as for eight SNPs, the pre-modern Korean people had a lactase non-persistent genotype. Our report contributes to the establishment of LNP associated SNP analysis technique that can be useful in forthcoming studies on human bones and mummy samples from East Asian archaeological sites. [ABSTRACT FROM AUTHOR]

Lactase persistence (LP) is a trait in which lactose can be digested throughout adulthood, while lactase non-persistence (LNP) can cause lactose intolerance and influence dairy consumption. One single nucleotide polymorphism (SNP ID: rs4988235) is often used as a predictor for dairy intake, since it is responsible for LP in people in European descent, and can occur in other ethnic groups. The objective of this study was to determine whether rs4988235 genotypes and ethnicity influence reported dairy consumption in the United States (U.S.). A food frequency questionnaire (FFQ) and multiple Automated Self-Administered 24-h recalls (ASA24®) were used to measure habitual and recent intake, respectively, of total dairy, cheese, cow's milk, plant-based alternative milk, and yogurt in a multi-ethnic U.S. cohort genotyped for rs4988235. Within Caucasian subjects, LP individuals reported consuming more recent total dairy and habitual total cow's milk intake. For subjects of all ethnicities, LP individuals consumed more cheese (FFQ p = 0.043, ASA24 p = 0.012) and recent total dairy (ASA24 p = 0.005). For both dietary assessments, Caucasians consumed more cheese than all non-Caucasians (FFQ p = 0.036, ASA24 p = 0.002) independent of genotype, as well as more recent intake of yogurt (ASA24 p = 0.042). LP subjects consumed more total cow's milk than LNP, but only when accounting for whether subjects were Caucasian or not (FFQ p = 0.015). Fluid milk and alternative plant-based milk consumption were not associated with genotypes or ethnicity. Our results show that both LP genotype and ethnicity influence the intake of some dairy products in a multi-ethnic U.S. cohort, but the ability of rs4988235 genotypes to predict intake may depend on ethnic background, the specific dairy product, and whether intake is reported on a habitual or recent basis. Therefore, ethnicity and the dietary assessment method should also be considered when determining the suitability of rs4988235 as a proxy for dairy intake.

Abstract Background Infantile colic is a common problem during the first three months of life. This randomized, double-blind, placebo-controlled trial conducted in an urban hospital in Delhi, India evaluated the efficacy and safety of oral lactase in management of infantile colic. Methods One hundred sixty-two clinically healthy infants aged 3 h/d; secondary outcomes were parental satisfaction and adverse events. Results At the end of four weeks, mean (SD) crying or fussing time (min/d) was significantly shorter in infants receiving lactase in comparison to placebo [89.9 (115.2) vs.178.5 (153.2); P = 0.001]. The mean (SD) number of days with colic was also significantly less in the lactase group as compared to placebo group at the end of the treatment [12.1 (7.8) vs 17.6 (8.4); P

Lactose intolerance is a common pathology that occurs due to the reduced activity of β-galactosidase leaving undigested lactose in the intestine. About 70% of the world population suffers from this condition. The gastro intestinal symptoms associated with this condition are diarrhoea, pain, nausea, bloating, flatulence, etc. It has been reported that these individuals are at a risk of developing several other pathologies like irritable bowel disease, osteoporosis, etc. Hence, proper diagnosis and treatment is essential for dealing with this condition. Various methods are used for providing an accurate diagnosis, such as hydrogen breath test (HBT), lactose intolerance test, genetic test, intestinal biopsy, etc. Depending on the type of intolerance, several methods are adopted for treating it, such as replacing enzyme, using exogenous enzymes, following lactose free diet, as well as consuming prebiotics and probiotics. Different methods are applied to synthesize lactose free dairy products to help lactose intolerant individuals suffering from important vitamins and minerals deprivation. Recently, plant-based milks are also used as a substitute for providing calcium and vitamins. The last few years have seen improvement in the quality and availability of lactose-free dairy products offering tempting foodstuffs to consumers. This narrative article aimed to review the existing science on lactose intolerance, along with its epidemiology, diagnosis, and clinical management.

The food enzyme β‐galactosidase (β‐D‐galactoside galactohydrolase, EC 3.2.1.23) is produced with the non‐genetically modified Kluyveromyces lactis strain GD‐YNL by Godo Shusei Co., Ltd. The food enzyme is intended to be used for the hydrolysis of lactose in milk processing, production of fermented milk products and whey processing. The food enzyme is also intended for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 54 mg TOS/kg body weight per day in European populations. As the production strain qualifies for the qualified presumption of safety approach of safety assessment and as no issue of concern raised from the production process, no toxicological studies other than assessment of allergenicity were necessary. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (EC 3.2.1.23) is produced with the non‐genetically modified Aspergillus sp. strain GD‐FAL by Godo Shusei Co., Ltd. The food enzyme is intended to be used in milk processing for the hydrolysis of lactose. The absence of viable cells of the production organism in the food enzyme was not demonstrated. Based on the assumption that all milk/dairy products are enzymatically treated, dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 0.301 mg TOS/kg body weight per day in European populations. The data provided did not allow concerns of genotoxicity of the food enzyme to be excluded. The systemic toxicity could not be assessed in the absence of an appropriate repeated dose 90‐day oral toxicity study. Consequently, a margin of exposure was not calculated. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. Based on the remaining concerns on genotoxicity, the inadequacies of the 90‐day repeated dose oral toxicity study in rats and the missing data regarding the absence of viable cells of the production strain in the food enzyme, the Panel could not conclude on the safety of this food enzyme. [ABSTRACT FROM AUTHOR]

Background Probiotics may alleviate lactose maldigestion. Objectives The objective was to select a probiotic with high lactase activity and compare it with lactase and placebo in clinical trials. Methods Bacterial cultures were screened for lactase activity in a model of the upper gastrointestinal (GI) tract. Bifidobacterium animalis subsp. lactis Bi-07 (Bi-07) counts were adjusted in subsequent experiments to correspond to 4500 Food Chemicals Codex (FCC) units of lactase, the amount in the European Food Safety Authority (EFSA)-approved health claim. Two crossover clinical trials, Booster Alpha and Booster Omega, were performed in participants with lactose intolerance, where 2 × 1012 CFUs Bi-07, 4662 FCC lactase, or placebo was consumed simultaneously with a lactose challenge, with 1-wk washouts between challenges. The trial designs were identical except for the source of lactose. Breath hydrogen concentration (BHC) was measured to assess the effect of the investigational products on lactose digestion, for which incremental area under the curve (iAUC) was the primary outcome. Peak BHC, cumulative BHC, and GI symptoms were secondary outcomes. Results Bi-07 was superior to placebo in reducing BHC [iAUC, parts per million (ppm) ∙ h] in both trials (Booster Alpha: geometric least square mean ratio: 0.462; 95% CI: 0.249, 0.859; P =  0.016; Booster Omega: 0.227; 95% CI: 0.095, 0.543; P  = 0.001). Lactase was superior to placebo in Booster Alpha (0.190; 95% CI: 0.102, 0.365; P  < 0.001) but not Booster Omega (0.493; 95% CI: 0.210, 1.156; P  = 0.102). Noninferiority of Bi-07 compared with lactase was observed in Booster Omega (0.460; 95% CI: 0.193, 1.096; P  = 0.079; CI upper limit < 1.25 noninferiority margin). Odds of abdominal pain (compared with placebo: 0.32, P  = 0.036) and flatulence (compared with placebo: 0.25, P  = 0.007) were lower with lactase in Booster Alpha. Increased odds of nausea were seen with Bi-07 (compared with placebo: 4.0, P  = 0.005) in Booster Omega. Conclusions Bi-07 has high lactase activit y , and in 2 clinical trials, it supported lactose digestion in individuals with lactose intolerance. These trials were registered at clinicaltrials.gov as NCT03659747 (Booster Alpha) and NCT03814668 (Booster Omega). [ABSTRACT FROM AUTHOR]

Introduction. The growth of gastrointestinal diseases associated with gastroesophageal reflux disease (GERD) dictates the need to develop methodological approaches for early outpatient diagnosis of comorbid gastrointestinal conditions using generally available methods, including transabdominal ultrasound (USR).Aim. To determine significant sonographic parameters of colon lesions in patients with polymorbid GERD, associated with clinical and metabolic concomitant changes, in order to improve transsyndromic diagnosis at an outpatient appointment.Materials and methods. The study included 150 outpatients with GERD (60 men and 90 women) with an average age of 40.2 ± 3.1 years old. All patients underwent clinical and laboratory examination, esophagogastroduodenoscopy, colonoscopy, ultrasound of the gastrointestinal tract with the calculation of the volume of gastroesophageal (GE) refluctate.Results and discussion. In patients with GERD, the criteria reflecting the pathological conditions of the colon according to the data of colonoscopy and ultrasound had a direct correlation. Statistically significant relationships between ultrasound signs of lesions of various segments of the colon with gender, age of patients, body mass index, erosive reflex disease and the volume of GE refluctate, as well as with lactase and vitamin D deficiency, the presence of yeast-like fungi and an increase in the level of fecal calprotectin are shown.Conclusions. The practical significance of the work lies in the possibility of diagnosing morphofunctional disorders of the colon in GERD patients with comorbid gastrointestinal pathology, associated not only with the main, but also with concomitant diseases by the ultrasound technique at the place of medical care. Tuning of gastrointestinal sonography, aimed at the immediate integration of ultrasound images into the patient management plan, involves the expansion of transsyndromic diagnostics and the substantiation of therapeutic tactic at an outpatient appointment.

Abstract The food enzyme β‐galactosidase (β‐D‐galactoside galactohydrolase, EC 3.2.1.23) is produced with the non‐genetically modified Kluyveromyces lactis strain GD‐YNL by Godo Shusei Co., Ltd. The food enzyme is intended to be used for the hydrolysis of lactose in milk processing, production of fermented milk products and whey processing. The food enzyme is also intended for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 54 mg TOS/kg body weight per day in European populations. As the production strain qualifies for the qualified presumption of safety approach of safety assessment and as no issue of concern raised from the production process, no toxicological studies other than assessment of allergenicity were necessary. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

In humans the expression of lactase changes during post-natal development, leading to phenotypes known as lactase persistence and non-persistence. Polymorphisms within the lactase gene (LCT) enhancer, in particular the -13910C > T, but also others, are linked to these phenotypes. We were interested in identifying dynamic mediators of LCT regulation, beyond the genotype at -13910C > T. To this end, we investigated two levels of lactase regulation in human intestinal samples obtained from New England children and adolescents of mixed European ancestry: differential expression of transcriptional regulators of LCT, and variations in DNA methylation, and their relation to phenotype. Variations in expression of CDX2, POU2F1, GATA4, GATA6, and HNF1α did not correlate with phenotype. However, an epigenome-wide approach using the Illumina Infinium HM450 bead chip identified a differentially methylated position in the LCT promoter where methylation levels are associated with the genotype at -13910C > T, the persistence/non-persistence phenotype and lactase enzymatic activity. DNA methylation levels at this promoter site and CpGs in the LCT enhancer are associated with genotype. Indeed, taken together they have a higher power to predict lactase phenotypes than the genotype alone.

The production of lactose-free yoghurts as a dietary product for people with milk sugar intolerance requires its extraction, which can affect the sensory and physicochemical properties of the finished product, thus, their evaluation to improve the technology is relevant. The purpose of the work was to explore yoghurts produced by conventional and lactose-free technologies. The object of the study was organic drinking yoghurt with “blueberry” filler (with probiotic) 2.5% and lactose-free organic yoghurt (with probiotic) 2.5%. The experimental samples were determined by a group of tasters organoleptic indicators, and titrated acidity and active acidity, conditional viscosity and structural and mechanical parameters of the product. According to the results of the research, organic drinking yoghurt with blueberry filler tasted sour-milk, without foreign flavours and odours, moderately sweet, with a pronounced taste of “blueberry” filler, consistency – homogeneous, tender, dense, without gas generation, with fresh blueberry particles distributed throughout the yoghurt, colour – with a shading characteristic of blueberries. Organic lactose-free yoghurt had a sour taste, fermented milk, without foreign flavours and odours, and colour – white. According to the results of physicochemical studies of the experimental samples of organic drinking yoghurt with “blueberry” filling and lactose-free organic yoghurt, it was established that the titrated acidity was 80 and 85o T, pH was 4.7 and 4.5, respectively. The mass fraction of carbohydrates in drinking yoghurt with the “blueberry” filling was 9.8 g/100g compared to 4.4 g/100g in lactose-free yoghurt, including sugar, respectively – 5.8 and 0 g/100 g. The energy value and caloric content were higher in the yoghurt sample with “blueberry” filling. The conditional viscosity of the test samples was respectively 1 min. 30 sec. and 59 sec. The degree of syneresis in the samples of organic drinking yoghurt with “blueberry” filling and lactose-free organic yoghurt was 55 and 45%, moisture content was 44.07 and 39.49%, respectively. The results obtained are relevant for understanding the changes in the properties of lactose-free yoghurts compared to the conventional type of this fermented milk product

Lactose intolerance is an important factor restricting the consumption of dairy products. Lactase is used to hydrolyze lactose in milk while generating galactooligosaccharides (GOS), thereby reducing the incidence of lactose intolerance. We used cow milk as raw materials, and selected enzyme preparations with high lactose hydrolysis rate and strong GOS generation ability from 14 commercially available lactase enzymes. The lactose hydrolysis rate is 5.85%-81.38%, and the GOS content is 0.03 g/L- 13.10 g/L. The mixing experiment design determined the two lactase enzymes (E10 and E11) ratio and the optimal enzymatic hydrolysis process of low-lactose prebiotic milk: compound lactases (E10:E11=0.756:0.244) addition 0.11%, 55℃for 5h, lactose hydrolysis rate and GOS content were 98.02% and 19.69g/L, respectively, and the remaining lactose content was about 0.97 g/L.

Abstract The food enzyme β‐galactosidase (EC 3.2.1.23) is produced with the non‐genetically modified Aspergillus sp. strain GD‐FAL by Godo Shusei Co., Ltd. The food enzyme is intended to be used in milk processing for the hydrolysis of lactose. The absence of viable cells of the production organism in the food enzyme was not demonstrated. Based on the assumption that all milk/dairy products are enzymatically treated, dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 0.301 mg TOS/kg body weight per day in European populations. The data provided did not allow concerns of genotoxicity of the food enzyme to be excluded. The systemic toxicity could not be assessed in the absence of an appropriate repeated dose 90‐day oral toxicity study. Consequently, a margin of exposure was not calculated. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. Based on the remaining concerns on genotoxicity, the inadequacies of the 90‐day repeated dose oral toxicity study in rats and the missing data regarding the absence of viable cells of the production strain in the food enzyme, the Panel could not conclude on the safety of this food enzyme.

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Kluyveromyces lactis strain KLA by DSM Food Specialties B.V. The genetic modifications did not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA. The food enzyme is intended to be used for the lactose hydrolysis in milk processing, production of fermented milk products and whey processing. It is also intended for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 11.876 mg TOS/kg body weight per day in European populations. The production strain of the food enzyme fulfils the requirements for the Qualified Presumption of Safety (QPS) approach to safety assessment. As no concerns arising from its genetic modification or from the manufacturing process have been identified, the Panel considered that toxicological tests are not needed for the assessment of this food enzyme. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. The Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Kluyveromyces lactis strain GAL by DSM Food Specialties B.V. It is intended to be used for the lactose hydrolysis in milk processing, production of fermented milk products and whey processing. It is also intended to be used for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme‐total organic solids (TOS) was estimated to be up to 10.78 mg TOS/kg body weight per day in European populations. As the production strain of K. lactis strain GAL qualifies for the Qualified Presumption of Safety (QPS) approach to safety assessment and no issue of concern arose from the production process, no toxicological data are required. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the Aspergillus oryzae strain GL 470 by Shin Nihon Chemical Co., Ltd. The food enzyme is free from viable cells of the production organism. It is intended to be used in five food manufacturing processes; lactose hydrolysis in milk processing, production of fermented milk products, whey processing, manufacture of enzyme‐modified dairy ingredients and in the manufacture of galacto‐oligosaccharides. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 1.388 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of repeated dose 90‐day oral toxicity studies in rats. The Panel identified a no observed adverse effect level of 7,000 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, results in a margin of exposure of at least 5,043. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel concluded that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered to be low. Based on the data provided and considering the most recent complete toxicological data set, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (β‐D‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Aspergillus niger strain TOL by DSM Food Specialties B.V. The genetic modifications did not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and recombinant DNA. The food enzyme is intended to be used in whey processing. Dietary exposure to the food enzyme total organic solids (TOS) was estimated to be up to 0.197 mg TOS/kg body weight (bw) per day in European populations. The toxicity studies were carried out with an asparaginase from A. niger strain ASP. The Panel considered this food enzyme as a suitable substitute for the β‐galactosidase to be used in the toxicological studies, because the genetic differences between the production strains are not expected to result in a different toxigenic potential and the raw materials and manufacturing processes of both food enzymes are comparable. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,038 mg TOS/kg bw per day, the highest dose tested. This results in a margin of exposure of at least 5,269. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Aspergillus oryzae strain AE‐LA by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. The food enzyme is intended to be used for lactose hydrolysis in milk processing, production of fermented milk products, whey processing and the manufacture of enzyme‐modified dairy ingredients. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 1.651 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,656 mg TOS/kg bw per day, the highest dose tested. This results in a margin of exposure of at least 1,003. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is considered to be low. Based on the data provided, the Panel concludes that this food enzyme does not give rise to safety concerns under the intended conditions of use. [ABSTRACT FROM AUTHOR]

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Aspergillus oryzae strain AE‐LA by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. The food enzyme is intended to be used for lactose hydrolysis in milk processing, production of fermented milk products, whey processing and the manufacture of enzyme‐modified dairy ingredients. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 1.651 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,656 mg TOS/kg bw per day, the highest dose tested. This results in a margin of exposure of at least 1,003. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is considered to be low. Based on the data provided, the Panel concludes that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Abstract The food enzyme β‐galactosidase (β‐D‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Aspergillus niger strain TOL by DSM Food Specialties B.V. The genetic modifications did not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and recombinant DNA. The food enzyme is intended to be used in whey processing. Dietary exposure to the food enzyme total organic solids (TOS) was estimated to be up to 0.197 mg TOS/kg body weight (bw) per day in European populations. The toxicity studies were carried out with an asparaginase from A. niger strain ASP. The Panel considered this food enzyme as a suitable substitute for the β‐galactosidase to be used in the toxicological studies, because the genetic differences between the production strains are not expected to result in a different toxigenic potential and the raw materials and manufacturing processes of both food enzymes are comparable. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of a repeated dose 90‐day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,038 mg TOS/kg bw per day, the highest dose tested. This results in a margin of exposure of at least 5,269. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the Aspergillus oryzae strain GL 470 by Shin Nihon Chemical Co., Ltd. The food enzyme is free from viable cells of the production organism. It is intended to be used in five food manufacturing processes; lactose hydrolysis in milk processing, production of fermented milk products, whey processing, manufacture of enzyme‐modified dairy ingredients and in the manufacture of galacto‐oligosaccharides. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 1.388 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not raise a safety concern. The systemic toxicity was assessed by means of repeated dose 90‐day oral toxicity studies in rats. The Panel identified a no observed adverse effect level of 7,000 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, results in a margin of exposure of at least 5,043. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel concluded that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is considered to be low. Based on the data provided and considering the most recent complete toxicological data set, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the non‐genetically modified Kluyveromyces lactis strain GAL by DSM Food Specialties B.V. It is intended to be used for the lactose hydrolysis in milk processing, production of fermented milk products and whey processing. It is also intended to be used for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme‐total organic solids (TOS) was estimated to be up to 10.78 mg TOS/kg body weight per day in European populations. As the production strain of K. lactis strain GAL qualifies for the Qualified Presumption of Safety (QPS) approach to safety assessment and no issue of concern arose from the production process, no toxicological data are required. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

Abstract The food enzyme β‐galactosidase (β‐d‐galactoside galactohydrolase; EC 3.2.1.23) is produced with the genetically modified Kluyveromyces lactis strain KLA by DSM Food Specialties B.V. The genetic modifications did not give rise to safety concerns. The food enzyme was considered free from viable cells of the production organism and its DNA. The food enzyme is intended to be used for the lactose hydrolysis in milk processing, production of fermented milk products and whey processing. It is also intended for lactose hydrolysis in milk products at home. Dietary exposure to the food enzyme–total organic solids (TOS) was estimated to be up to 11.876 mg TOS/kg body weight per day in European populations. The production strain of the food enzyme fulfils the requirements for the Qualified Presumption of Safety (QPS) approach to safety assessment. As no concerns arising from its genetic modification or from the manufacturing process have been identified, the Panel considered that toxicological tests are not needed for the assessment of this food enzyme. A search for similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood for this to occur is low. The Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.

With increasing health awareness worldwide, lactose intolerance has become a major concern of consumers, creating new market opportunities for low-lactose/lactose-free dairy foods. In recent years, through innovating processes and technologies, dairy manufacturers have significantly improved the variety, and functional and sensory qualities of low-lactose and lactose-free dairy products. Based on this, this paper first covers the pathology and epidemiology of lactose intolerance and market trends. Then, we focus on current advantages and disadvantages of different lactose hydrolysis technologies and improvements in these technologies to enhance nutritional value, and functional, sensory, and quality properties of lactose-free dairy products. We found that more and more cutting-edge technologies are being applied to the production of lactose-free dairy products, and that these technologies greatly improve the quality and production efficiency of lactose-free dairy products. Hopefully, our review can provide a theoretical basis for the marketing expansion and consumption guidance for low-lactose/lactose-free dairy products.

Background: Infantile colic is a common problem during the first three months of life. This randomized, double-blind, placebo-controlled trial conducted in an urban hospital in Delhi, India evaluated the efficacy and safety of oral lactase in management of infantile colic.Methods: One hundred sixty-two clinically healthy infants aged < 5 months age [mean (SD) = 63.5 (30.5) days] fulfilling the Rome-IV diagnostic criteria for infantile colic were enrolled. Eligible children were randomly allocated to receive 5 drops of lactase (600 FCC units/mL) (n = 80) or placebo (n = 82) mixed with breast milk or formula feed four times a day for a duration of 4 weeks. Primary outcomes were duration of crying or fussing (min/d), and number of days with colic lasting > 3 h/d; secondary outcomes were parental satisfaction and adverse events.Results: At the end of four weeks, mean (SD) crying or fussing time (min/d) was significantly shorter in infants receiving lactase in comparison to placebo [89.9 (115.2) vs.178.5 (153.2); P = 0.001]. The mean (SD) number of days with colic was also significantly less in the lactase group as compared to placebo group at the end of the treatment [12.1 (7.8) vs 17.6 (8.4); P < 0.001]. By the end of 4th week, parental satisfaction in terms of infant's mood, activity, alertness, comfort and oral intake was better in intervention group. The adverse event profile was comparable between two groups.Conclusions: Oral lactase treatment in infantile colic results in symptomatic relief in terms of shortening of duration of crying or fussing, and better parental satisfaction.Trial Registration: Clinical trial registry of India (CTRI/2017/12/010930) registered on 20/12/2017. [ABSTRACT FROM AUTHOR]