Search

Rambutan seeds are by-products generated from fruit-processing factories; the leftover seeds are buried in landfills, generating methane emissions. This work aimed to extract polysaccharides (POLS) from rambutan seeds by using subcritical water extraction (SWE). The effects of defatting pretreatment and operating parameters in SWE were investigated using a Box–Behnken design. The results show that defatting pretreatment significantly enriched the POLS yield, while it had no significant effect on the total sugar content. Using the desirability approach, the suitable feedstock for SWE was defatted rambutan seeds. The maximum desirability of 0.86 was found at a temperature range of 145–150 °C, an extraction time of 15 min, and a liquid–solid ratio of 10:1. The POLS yield and total sugar content were in the range of 52.33–55.63 g/100 g feedstock and 83.37–87.45 g/100 g POLS, respectively. The extracted POLS had an equivalent molecular weight of 413.70 kDa that could be used as an extender in plant-based products. In conclusion, the defatting pretreatment of rambutan seeds not only improved the POLS yield obtained via SWE but also generated additional lipids that could be utilized as an unconventional source of specialty fat. [ABSTRACT FROM AUTHOR]

This paper presents the initial exploration of the free radical scavenging capabilities of peptides derived from protein hydrolysates (PPH) obtained from Zingiber cassumunar rhizomes (Phlai). To replicate the conditions of gastrointestinal digestion, a combination of pepsin and pancreatin proteolysis was employed to generate these hydrolysates. Subsequently, the hydrolysate underwent fractionation using molecular weight cut-off membranes at 10, 5, 3, and 0.65 kDa. The fraction with a molecular weight less than 0.65 kDa exhibited the highest levels ABTS, DPPH, FRAP, and NO radical scavenging activity. Following this, RP-HPLC was used to further separate the fraction with a molecular weight less than 0.65 kDa into three sub-fractions. Among these, the F5 sub-fraction displayed the most prominent radical-scavenging properties. De novo peptide sequencing via quadrupole-time-of-flight-electron spin induction-mass spectrometry identified a pair of novel peptides: Asp-Gly-Ile-Phe-Val-Leu-Asn-Tyr (DGIFVLNY or DY-8) and Ile-Pro-Thr-Asp-Glu-Lys (IPTDEK or IK-6). Database analysis confirmed various properties, including biological activity, toxicity, hydrophilicity, solubility, and potential allergy concerns. Furthermore, when tested on the human adenocarcinoma colon (Caco-2) cell line, two synthetic peptides demonstrated cellular antioxidant activity in a concentration-dependent manner. These peptides were also assessed using the FITC Annexin V apoptosis detection kit with PI, confirming the induction of apoptosis. Notably, the DY-8 peptide induced apoptosis, upregulated mRNA levels of caspase-3, -8, and -9, and downregulated Bcl-2, as confirmed by real-time quantitative polymerase chain reaction (RT-qPCR). Western blot analysis indicated increased pro-apoptotic Bax expression and decreased anti-apoptotic Bcl-2 expression in Caco-2 cells exposed to the DY-8 peptide. Molecular docking analysis revealed that the DY-8 peptide exhibited binding affinity with Bcl-2, Bcl-xL, and Mcl-1, suggesting potential utility in combating colon cancer as functional food ingredients. [ABSTRACT FROM AUTHOR]

The purpose of this study is to assess the bioactive peptides derived from the defatted lemon basil seeds hydrolysate (DLSH) for their ability to inhibit pancreatic lipase, decrease intracellular lipid accumulation, and reduce adipogenesis. Response surface methodology (RSM) was employed to optimize trypsin hydrolysis conditions for maximizing lipase inhibitory activity (LI). A hydrolysis time of 387.06 min, a temperature of 49.03°C, and an enzyme concentration of 1.61% w/v, resulted in the highest LI with an IC50 of 368.07 μg/mL. The ultrafiltration of the protein hydrolysate revealed that the fraction below 0.65kDa exhibited the greatest LI potential. Further purification via RP-HPLC identified the Gly-Arg-Ser-Pro-Asp-Thr-His-Ser-Gly (GRSPDTHSG) peptide in the HPLC fraction F1 using mass spectrometry. The peptide was synthesized and demonstrated LI with an IC50 of 0.255 mM through a non-competitive mechanism, with a constant (Ki) of 0.61 mM. Docking studies revealed its binding site with the pancreatic lipase-colipase complex. Additionally, GRSPDTHSG inhibited lipid accumulation in 3T3-L1 cells in a dose-dependent manner without cytotoxic effects. Western blot analysis indicated downregulation of PPAR-γ and SREBP-1c levels under GRSPDTHSG treatment, while an increase in AMPK-α phosphorylation was observed, suggesting a role in regulating cellular lipid metabolism. Overall, GRSPDTHSG demonstrates potential in attenuating lipid absorption and adipogenesis, suggesting a prospective application in functional foods and nutraceuticals. [ABSTRACT FROM AUTHOR]

Rambutan seeds (RS) are industrial waste often generated in the canned fruit industry. The aim of this study was to extract polysaccharides from defatted rambutan seeds or crude polysaccharides (POLS-DRSs) with subcritical water. Defatted seed powder (DRS) was extracted by hot-water extraction (HWE) at 100 °C as a reference condition. Subcritical water extraction (SWE) was performed at 120–140 °C and an initial pressure of 2 MPa. A sample-to-water ratio of 1:10 (w/w) and an extraction time of 15–60 min were used for both methods. The results show that gravimetric extraction yields of 53.01 g/100 g DRS and 7.71–41.70 g/100 g DRS were obtained from HWE and SWE, respectively. Additionally, HWE provided a total sugar content of 30.75 g/100 g POLS-DRSs, while SWE generated a total sugar content in the range of 27.00–49.76 g/100 POLS-DRSs. The antioxidant activities of POLS-DRSs were measured with a 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging assay. An amount of 40 mg of POLS-DRSs obtained at 120 °C after 60 min provided the highest DPPH activity of 82.93% inhibition. The POLS-DRSs were suitable for growing microorganisms because they had a high sugar content and a low total phenolic content. A prebiotic activity assay will be carried out in future studies. [ABSTRACT FROM AUTHOR]

Spent coffee grounds (SCGs) are currently considered abandoned landfill waste despite retaining valuable organic compounds, especially with a high protein content of 16.64 ± 0.13 g/g dried SCGs and a high oil content of 15.48 ± 0.17 g/g dried SCGs. As a result, SCGs could serve as a potential source of valuable ingredients. However, utilizing a single technical strategy of alternative green extractions was insufficient for extracting the target compounds and hydrolyzing proteins. This work aimed to optimize the operating parameters of enzyme-assisted extraction (EAE), microwave-assisted extraction (MAE), and subcritical water extraction (SWE) using a response surface methodology. The results showed that EAE, at a papain-to-substrate ratio (E/S) of 0.5 and a duration of 15 min, generated a %DH of 93.39% and provided a water soluble protein concentration (WSPC) in the range of 400 to 800 µg/mL. Moreover, MAE provided a maximum %DH of 9.72% at 600 watts and 10 min, while SWE produced a maximum %DH of 13.41% at 160 °C in 17.5 min. However, the WSPCs of MAE and SWE extracts were comparable at ~250 µg/mL. The combination MAE−SWE enhanced the %DH of hydrolysates by more than the combined SWE−MAE, SWE, and MAE. However, the effects of differential hydrolysis on bioactivity are not directly correlated with %DH. In this study, the highest antioxidant activity was found at an E/S of 0.5 and in 15 min for EAE, at 350 W and in 10 min for MAE, and at 160 °C and in 30 min for SWE. This work demonstrated that the valorization of SCGs not only reduces the amount of waste but also yields functional cosmeceutical and nutraceutical ingredients. [ABSTRACT FROM AUTHOR]

When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors. [ABSTRACT FROM AUTHOR]

Abstract Background The similarly in plant physiology and the difficulty of plant classification, in some medicinal plant species, especially plants of the Zingiberaceae family, are a major problem for pharmacologists, leading to mistaken use. To overcome this problem, the proteomic base method was used to study protein profiles of the plant model, Curcuma comosa Roxb., which is a member of the Zingiberaceae and has been used in traditional Thai medicine as an anti-inflammatory agent for the treatment of postpartum uterine bleeding. Results Due to the complexity of protein extraction from this plant, microscale solution-phase isoelectric focusing (MicroSol-IEF) was used to enrich and improve the separation of Curcuma comosa rhizomes phenol-soluble proteins, prior to resolving and analyzing by two-dimensional polyacrylamide gel electrophoresis and identification by tandem mass spectrometry. The protein patterns showed a high abundance of protein spots in the acidic range, including three lectin proteins. The metabolic and defense enzymes, such as superoxide dismutase (SOD) and ascorbate peroxidase, that are associated with antioxidant activity, were mainly found in the basic region. Furthermore, cysteine protease was found in this plant, as had been previously reported in other Zingiberaceae plants. Conclusion This report presents the protein profiles of the ginger plant, Curcuma comosa. Several interesting proteins were identified in this plant that may be used as a protein marker and aid in identifying plants of the Zingiberaceae family.

Bee pollen protein was hydrolyzed using the commercial Alcalase, Flavourzyme and Neutrase enzymes. The Neutrase hydrolysate formed from a 1:1 (v/v) enzyme/substrate ratio (NH1) showed the highest nitric oxide (NO) radical scavenging activity. The NH1 was further separated into five fractions based on molecular weight (MW1–5) and MW1, the smallest weight fraction (< 0.65 kDa), possessed the highest NO inhibitory activity. The effects of NH1 on the production of NO were assessed by incubating with lipopolysaccharide-stimulated RAW264.7 macrophage cells. NO levels from the culture supernatants were determined by the Griess reaction. The results showed that MW1 suppressed the production of pro-inflammatory cytokines including cyclooxygenase-2 (COX-2), inducible nitric oxide synthase (iNOS), tumor interleukin-6 (IL-6) and necrosis factor transcript expression (TNF-α) in RAW264.7 macrophage cells. Thus, the MW1 fraction was fractionated using reversed-phase high-performance liquid chromatography into six principal fractions (H1–6), where H2, H3 and H4 showed strong NO inhibitory activity. Seven peptide sequences were obtained by quadrupole time-of-flight mass spectrometry, three of which displayed potent anti-inflammatory activity and may be useful ingredients in functional food and pharmaceutical drugs. [ABSTRACT FROM AUTHOR]

The Synechococcus sp. VDW peptides were prepared by trypsin digestion, which was then purified by ultrafiltration with molecular weight cut off membranes of 10, 5 and 3 kDa. Among the fractions, the MW <3 kDa fraction exhibited high levels of inhibitory activity toward the NO radical scavenging activities with IC50 values of 34.51 ± 9.8 μg/mL. The MW <3 kDa fraction was purified by reversed-phase HPLC to yield four fractions. The 30–40 min sub-fraction with maximum NO radical scavenging activity (77.50 ± 0.55%) was selected for further analysis by Q-TOF ESI mass spectrometry. Five isolated peptides with amino acid sequences of AILQSYSAGKTK; 1,265.69 Da, ALNKTHLIQTK; 1,265.74 Da, LLVHAPVK; 875.55 Da, IPDAHPVK; 875.48 Da, and VVVLRDGAVQQLGTPR; 1,706.97 Da were identified. The MW <3 kDa fraction showed no cytotoxicity toward RAW264.7 macrophage cells. Quantitative RT-PCR results showed that the MW <3 kDa fraction reduced gene expression of pro-inflammatory cytokines iNOS, TNF-α, COX-2, and IL-6. The peptides isolated from the MW <3 kDa fractions represent potential model peptides to develop natural anti-inflammation food-grade ingredients, drugs, and cosmetic products. [ABSTRACT FROM AUTHOR]

BACKGROUND Salmon bones, a waste by‐product from the salmon industry, were used as a protein hydrolysate source for the production of bioactive peptides. The aim of this work was to evaluate the potential antioxidant and anti‐inflammatory properties of salmon bone protein hydrolysate (SBPH). RESULTS: Salmon bones were hydrolyzed by separately using one of four proteases (Alcalase, Favourzyme, Neutrase and papain) at various concentrations (10, 25 and 50 mg mL−1), where the SBPH derived from 10 mg mL−1 papain hydrolysis exhibited the highest nitric oxide (NO) radical scavenging activity. After ultrafiltration, the MW < 0.65 kDa fraction showed the strongest NO inhibitory activity and was further fractionated by gel filtration chromatography (G1 and G2 fractions) and reverse‐phase high‐performance liquid chromatographic fractionation of the G1 fraction, from which the three main peaks (H1, H2 and H3) were found to have a marked NO‐inhibitory activity and their peptide sequences were determined. Moreover, the G1 fraction was shown to inhibit both the lipopolysaccharide (LPS)‐induced NO production and the LPS‐induced inducible NO synthase , interleukin‐6, tumor necrosis factor‐α and induced NO production and the LPSCOX‐2 mRNA levels in RAW 264.7 cells. CONCLUSIONS: Salmon bones from the salmon fisheries and farming industry were utilized by enzymatic hydrolysis for the production of valuable peptides. The results of this study suggested that bioactive peptides derived from salmon bones would be alternative anti‐inflammation materials in functional resources. © 2019 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Copyright of Food Technology & Biotechnology is the property of Food Technology & Biotechnology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Lychee (Litchi chinensis) seeds, a by-product from the canned lychee processing, were hydrolyzed using various concentrations of proteases (Alcalase, Flavourzyme, and Neutrase). The protein hydrolysate produced with Neutrase at a concentration of 50 mg/mL exhibited the highest free radical scavenging activity. After ultrafiltration, the fraction containing peptides of less than 650 Da was purified by using gel filtration chromatography into G1-G3. The G1 fraction exhibited the highest activity and was further purified by reversed phase high performance liquid chromatography (RP-HPLC). Four fractions (H1-H4) were isolated and exhibited efficient nitric oxide (NO) scavenging activity. The G1 fraction inhibited NO production in lipopolysaccharide (LPS) stimulated RAW 264.7 cells with down-regulation of inducible nitric oxide synthase (iNOS) and interleukin-6 (IL-6). The results showed that lychee seed peptide hydrolysates exhibited potent anti-inflammatory activities, suggesting the peptides may be useful as additives to health products such as functional foods and/or pharmaceuticals. [ABSTRACT FROM AUTHOR]

The metabolic responses of Aspergillus terreus NRRL1960 to stress conditions (low dissolved oxygen and pH with limited nitrogen and phosphate) in the two-phase fermentation were investigated in this study. The fermentation kinetics suggested that itaconate production was suppressed under low dissolved oxygen (DO) concentrations. A slight change in pH caused a significant change in itaconate production. The transcriptomic data revealed that under low DO concentration, the glycolytic pathway was uncoupled from the oxidative phosphorylation, resulting in the activation of substrate-level phosphorylation as an alternative route for ATP regeneration. The downregulation of pdh genes, the genes encoding ATP synthase and succinate dehydrogenase, confirmed the observation of the uncoupling of the oxidative TCA cycle from glycolysis. It was found that the upregulation of pyc resulted in a large pool of oxaloacetate in the cytosol. This induced the conversion of oxaloacetate to malate. The upregulation of the gene encoding fumarate hydratase with the subsequent formation of fumarate was found to be responsible for the regeneration of NADPH and ATP under the condition of a low dissolved oxygen level. The large pool of oxaloacetate drove itaconic acid production also via the oxidative TCA cycle. Nevertheless, the downregulation of ATP synthase genes resulted in the deficiency of the proton-pumping H+ ATPase and the subsequent stress due to the failure to maintain the physiological pH. This resulted in itaconate production at a low titer. The fermentation kinetics and the transcriptomic data provided in this study can be used for further process optimization and control to improve itaconate production performance. [ABSTRACT FROM AUTHOR]

Defatted rice bran (DRB) is a by-product of oil extraction from rice bran ( Oryza sativa L.), and has health benefits. This in vitro study investigated the antioxidant and anti-inflammatory effects of four crude DRB protein hydrolysate fractions prepared by pepsin-pancreatin digestion and fractionated by ultrafiltration on a transformed macrophage cell line, RAW264.7. Protein hydrolysates with MW <3 kDa (F4 fraction) had the lowest IC50 for NO-, DPPH˙ and ABTS radical scavenging activities (0.38 ± 0.01, 1.24 ± 0.03 and 0.17 ± 0.01 µg/mL, respectively). The pooled fraction formed after Reverse phase-High-performance liquid chromatography (HPLC) (F4-5) had the highest percentage inhibition of radical scavenging for DPPH˙, and NO- (25.04 ± 0.88, and 6.50 ± 0.39%, respectively). LC-MS of F4-5 revealed peptides exhibiting antioxidant activity were composed of His (H), Trp (W) and Tyr (Y) that known to enhance the scavenging activities of peptides. The F4 fraction suppressed lipopolysaccharide and rmIFN-γ mediated increase in iNOS, IL-6 and TNF-α mRNA levels in RAW264.7 cells, suggesting the interference was mediated at the transcriptional level. Practical Application Defatted rice bran (DRB) is a good source of nutritional proteins. In this study, DRB protein was hydrolyzed using proteases and further fractionated by ultrafiltration. The results demonstrated that DRB hydrolysates and their fractions exhibited antioxidant and anti-inflammatory activities indicating these as a potential source of functional food and medicines. [ABSTRACT FROM AUTHOR]

Plant proteins have been investigated for their antioxidant activities, but there are still no reports detailing the antioxidant activity levels of plants in the Zingiberaceae family, which are popular food agents and used in folklore medicine. In this study, the crude rhizome protein extract and associated pepsin/pancreatin protein hydrolysate of 15 plants in the Zingiberaceae family were screened using the DPPH method for antioxidant activity. The protein hydrolysate of C. zedoaria possessed the highest antioxidant activity (IC50 of 25.7±6.3μg/mL), which was close to that of the reference ascorbic acid (IC50 of 22.3±1.8μg/mL). After enrichment by Q Sepharose ion exchange chromatography using a five step elution gradient of increasing NaCl concentration (0, 0.25, 0.5, 0.75 and 1M), the fraction eluting in the 0.5M NaCl (F50) showed the highest antioxidant activity (IC50 of 41.78±2.9μg/mL), and was found to have weak in vitro cytotoxicity against the HEP-G2 and SW620 cell lines (IC50 of 200.8±11.8 and 241.0±9.3μg/mL, respectively), but not the BT474, CHAGO and KATO-3 cell lines. F50 had an estimated molecular weight by MALDI-TOF mass spectrometry of 12,400-12,800 Da. [ABSTRACT FROM AUTHOR]