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Copyright of China Surfactant Detergent & Cosmetics (2097-2806) is the property of China Surfactant Detergent & Cosmetics Editorial Office 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.)

Enzymatic additives, particularly alkaline proteases, play a crucial role in enhancing detergent effectiveness against protein-based stains. Despite advancements in enzyme stabilization techniques, there is a need for innovative strategies to further improve protease stability in laundry detergents. However, research exploring the utilization of substrate imprinting technology to achieve this objective remains limited. Therefore, this study aims to enhance the stability of alkaline proteases in laundry detergents by employing casein as an imprinting substrate and utilizing transglutaminase-mediated (TGase) crosslinking to modify proteases 102 and 306. The optimal temperature, pH, and thermal stability of the modified alkaline proteases 102 and 306 showed no significant changes. However, these two modified alkaline proteases exhibited varying degrees of improvement in stability among the 14 detergent additives tested. Under 40 °C incubation for 24 h, the relative enzyme activity of modified alkaline protease 102 increased approximately 1.4–15-fold in AEO-9, BS-12, CMI, APG, FMEE, and SOE, while the relative enzyme activity of modified alkaline protease 306 increased approximately 1.2–3.7-fold across different additives (FMEE, AEO-9, BS-12, SOE, FAA, and AEC-9Na). These modified proteases demonstrated improved stability and wider applicability across commercial detergent formulations available. Integrated into standard laundry detergent at a 1:7 ratio before and after modification, they effectively removed protein stains from the cotton fabric after 24 h of 40 °C incubation. These findings provide insights into more effective stain-removal techniques. [ABSTRACT FROM AUTHOR]

This article presents a case report of a 74-year-old man who developed allergic contact dermatitis to benzisothiazolinone (BIT) in a laundry detergent. The man had been experiencing a pruritic rash for 8 years, which persisted despite changes in medication and furniture. Multiple skin biopsies showed inflammation. Patch testing revealed a positive reaction to BIT, and the patient's rash cleared after switching to a different laundry product. The article highlights the limited reports of laundry detergents causing allergic contact dermatitis and emphasizes the importance of identifying the ingredients in laundry detergents for individuals with dermatitis. [Extracted from the article]

Laundry detergents are mixtures of chemical compounds commonly used as cleaning agents for clothes and various objects. Their different degree of decomposition and transformation make wastewater to contain a variable proportion of such contaminants. There is a possibility of contamination of the soil, but also of plant crops with detergents, if these insufficiently treated waters are used in irrigation.The aim of this study is to evaluate the degree of phytotoxicity of lavender powder detergent on lettuce (Lactuca sativa L.). The effect of the detergent was highlighted through the germination of seeds and the growth of lettuce seedlings.The use of lettuce as a test plant is recommended by OECD 208 and is a species that can be easily handled in pilot conditions but also in the field. [ABSTRACT FROM AUTHOR]

Abstract Background Chicken feathers are the most abundant agro-wastes emanating from the poultry processing farms and present major concerns to environmentalists. Bioutilization of intractable feather wastes for the production of critical proteolytic enzymes is highly attractive from both ecological and biotechnological perspectives. Consequently, physicochemical conditions influencing keratinase production by Bacillus sp. CSK2 on chicken feathers formulation was optimized, and the keratinase was characterized. Results The highest enzyme activity of 1539.09 ± 68.14 U/mL was obtained after 48 h of incubation with optimized conditions consisting of chicken feathers (7.5 g/L), maltose (2.0 g/L), initial fermentation pH (5.0), incubation temperature (30 °C), and agitation speed (200 rpm). The keratinase showed optimal catalytic efficiency at pH 8.0 and a temperature range of 60 °C – 80 °C. The keratinase thermostability was remarkable with a half-life of above 120 min at 70 °C. Keratinase catalytic efficiency was halted by ethylenediaminetetraacetic acid and 1,10-phenanthroline. However, keratinase activity was enhanced by 2-mercaptoethanol, dimethyl sulfoxide, tween-80, but was strongly inhibited by Al3+ and Fe3+. Upon treatment with laundry detergents, the following keratinase residual activities were achieved: 85.19 ± 1.33% (Sunlight), 90.33 ± 5.95% (Surf), 80.16 ± 2.99% (Omo), 99.49 ± 3.11% (Ariel), and 87.19 ± 0.26% (Maq). Conclusion The remarkable stability of the keratinase with an admixture of organic solvents or laundry detergents portends the industrial and biotechnological significance of the biocatalyst.

Drought is the major challenge of the present century in agricultural areas. Water scarcity has led to the use of contaminatedwater. The objective of the studywas to determine the tolerance of wheat, Sirvan cultivar, to detergent contaminated water and drought at germination and early growth stages. The research included germination and pot experiments. In the germination experiment, laundry detergent concentrations of 0.05 g L-1, 0.5 g L-1, and 5 g L-1 were used to produce contaminated water and isoosmotic potential of polyethylene glycol (PEG) was used to produce water stress. In the pot experiment, the concentrations used in the germination experiment were applied with two irrigation intervals of 2 and 4 days. The results showed that at an osmotic potential of -0.217MPa of laundry detergent and PEG, all germination traits were drastically reduced, but radicle length and length-based seed vigor were reduced at an osmotic potential of -0.035 MPa of detergent. A laundry detergent concentration of 5 g L-1 combined with drought reduced plant height, leaf area, fresh weight of leaves and stems, and relative water content of leaves. The seed germination stage was more sensitive to the laundry detergent than the early growth stage. It is recommended to irrigate wheat (Sirvan variety) at the germination stage with water that is not contaminated with detergent. [ABSTRACT FROM AUTHOR]

Here we describe an in-house kit for high throughput DNA extraction using laundry detergent. A simplified lysis buffer made only from 0.08 M EDTA, 0.1 M Tris, and laundry powder is the core of our protocol. We extracted genomic DNA from 150 µL of whole blood collected from different farm animals and compared the performance to both the DNeasy Blood & Tissue Kit (Qiagen) and the widely used salting-out procedure. An evaluation of the concentration and quality of the extracted DNA was then assessed by the NanoDrop absorption spectra, agarose gel migration, amplification in PCR and the Sanger sequencing. The in-house kit successfully extracted clean DNA from all blood samples, and discernably outperformed the commercial kits and the original salting-out procedure in the sense of the simplicity, cost-efficiency, quantity, and the quality of purified DNA. Apart from replacing proteinase K and the sodium dodecyl sulfate treatment by the laundry detergent, our protocol instructs a lysis buffer that eliminates sucrose, Triton X-100, MgCl2, NH4Cl, and KCl. Our handmade kit might be of interest for laboratories in underdeveloped countries with a budget shortage or applications in difficult field conditions, for example, when fridge storage for proteinase K cannot be ensured. [ABSTRACT FROM AUTHOR]

Copyright of China Surfactant Detergent & Cosmetics (1001-1803) is the property of China Surfactant Detergent & Cosmetics Editorial Office 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.)

Background: Chicken feathers are the most abundant agro-wastes emanating from the poultry processing farms and present major concerns to environmentalists. Bioutilization of intractable feather wastes for the production of critical proteolytic enzymes is highly attractive from both ecological and biotechnological perspectives. Consequently, physicochemical conditions influencing keratinase production by Bacillus sp. CSK2 on chicken feathers formulation was optimized, and the keratinase was characterized. Results: The highest enzyme activity of 1539.09 ± 68.14 U/mL was obtained after 48 h of incubation with optimized conditions consisting of chicken feathers (7.5 g/L), maltose (2.0 g/L), initial fermentation pH (5.0), incubation temperature (30 °C), and agitation speed (200 rpm). The keratinase showed optimal catalytic efficiency at pH 8.0 and a temperature range of 60 °C – 80 °C. The keratinase thermostability was remarkable with a half-life of above 120 min at 70 °C. Keratinase catalytic efficiency was halted by ethylenediaminetetraacetic acid and 1,10-phenanthroline. However, keratinase activity was enhanced by 2-mercaptoethanol, dimethyl sulfoxide, tween-80, but was strongly inhibited by Al3+ and Fe3+. Upon treatment with laundry detergents, the following keratinase residual activities were achieved: 85.19 ± 1.33% (Sunlight), 90.33 ± 5.95% (Surf), 80.16 ± 2.99% (Omo), 99.49 ± 3.11% (Ariel), and 87.19 ± 0.26% (Maq). Conclusion: The remarkable stability of the keratinase with an admixture of organic solvents or laundry detergents portends the industrial and biotechnological significance of the biocatalyst. [ABSTRACT FROM AUTHOR]

Abstract Background European legislation has banned the preservative methylisothiazolinone (MI) from inclusion in leave-on cosmetics. However, the risk for allergic reactions depends on exposure. The aim of this study was to determine the risk of MI in laundry detergents for household machine washing. Methods Different formulations of laundry detergents with commercial MI levels, up to one thousand ppm were used and three different types of clothes were washed in a normal household machine setting one time and 10 times. The level of MI was measured by HPLC. Results While MI could be retrieved in the positive control of clothes drenched with washing powder but not washed afterwards, MI could not be detected in any specimen of clothes washed under household conditions. The detection limit was 0.5 ppm. Conclusion It is important to discuss the difference of risk and hazard. While MI clearly is a high hazard as a strong contact allergen, the risk depends on exposure. Regarding the risk of exposure levels for the consumer to MI in clothes it can be stated that the use of MI in laundry detergents is safe for the consumer if these products are used according to the instructions in the normal household setting machine wash.

For consumers who use laundry detergents, a top unmet need is to reduce malodor that can persist on fabrics, even after washing and drying. A known source of odor is autoxidation of residual sebum on fabric, leading to the generation of an array of odiferous compounds. To prevent this oxidation process, two technologies were evaluated: (i) antioxidants to scavenge radicals and (ii) metal chelants to inhibit the involvement of copper ions as catalysts in the autoxidation process. Copper is a common component of sweat, soil, and municipal water supplies, especially where copper piping is involved, which is typical in many US homes and businesses. For the evaluations, swatches of fabric were treated with artificial sebum, then washed in commercial washing machines with tap water containing laundry detergent, and dried using commercial dryers. Copper added to the wash at a level representative of consumer homes substantially increased the formation of known malodor molecules. Copper chelants [in particular, diethylenetriamine (DETA)] added to the wash were effective in inhibiting the formation of malodor molecules. In combination with antioxidants [in particular, methyl 3‐(3, 5‐di‐tert‐butyl‐4‐hydroxyphenyl)propanoate (MtBHPP)], the inhibitory effect was greater. Even at low concentrations (<1%), DETA and MtBHPP were effective at inhibiting the generation of known malodor molecules on fabrics. As DETA and MtBHPP meet performance, cost, and stability considerations, they hold promise for use in high‐quality commercial laundry detergent products designed to eliminate malodor on consumer fabrics. [ABSTRACT FROM AUTHOR]

A new serine alkaline protease (designated as SAPGB) from Gracilibacillus boraciitolerans strain LO15, was produced (9000 U/mL), purified, and characterized. SAPGB has a monomer structure with a precise molecular weight of 30,285.03 kDa as learnt from matrix-assisted laser desorption/ionization-time of flight/mass spectroscopy (MALDI-TOF/MS) exploration. The NH 2 -terminal amino-acid succession revealed significant identity with Bacillus proteases. The SAPGB was irreversibly inhibited by diiodopropyl fluorophosphates (DFP) and phenylmethylsulfonyl fluoride (PMSF). The enzyme displayed optimum activity at 65 °C and pH 10. The maximal activity was achieved in the range 0.5–5 M NaCl and about 52% of the activity was preserved across the broad salinity range of 0–30%. SAPGB exhibited a considerable catalytic efficiency (ratio k cat / K m) and degree of hydrolysis (DH). In addition, SAPGB showed a high tolerance to several organic solvents and an excellent detergent compatibility than SAPV, SAPA, Thermolysin type X, and Esperase 8.0 L. These properties make SAPGB a potential candidate for detergent formulations. On the other hand, sapGB gene was cloned and expressed in E. coli BL21(DE3)pLysS and the biochemical properties of the purified extracellular recombinant protease (rSAPGB) were similar to those of SAPGB. Finally, a 3D structural model of SAPGB was constructed by homology modeling. Unlabelled Image • The protease SAPGB from Gracilibacillus boraciitolerans strain LO15 was purified and typified. • The optimum pH and temperature values for activity were pH 10 and 65 °C, respectively. • The sapGB gene encoding SAPGB, was cloned, sequenced, and expressed in E. coli BL21(DE3)pLysS. • Pro-SAPGB 3D-structure model was built using structure of Pro-subtilisin E (PDB ID: 3WHI). • The SAPGB enzyme is a potential candidate for peptide synthesis and detergent formulations. [ABSTRACT FROM AUTHOR]

Laundry detergents are chemicals widely used in everyday life, and in numerous industry branches. In order to perceive the radiological aspect of environmental pollution by wastewater, the analysis of laundry detergents available on the Serbian market was undertaken. Laundry detergent samples were measured by means of gamma spectrometry and the results are presented in this paper. Analysis of the obtained activity concentrations showed that laundry detergents in Serbia mostly fulfill the international recommendation and requirements regarding the phosphate content. Besides that, the content of the detected radionuclides in laundry detergent samples indicates the minor radiological risk to the environment via wastewaters. [Project of the Serbian Ministry of Education, Science and Technological Development, Grant no. 171018]

Summary: Chemical catalysts are being replaced by biocatalysts in almost all industrial applications due to environmental concerns, thereby increasing their demand. Enzymes used in current industries are produced in microbial systems or plant seeds. We report here five newly launched leaf‐enzyme products and their validation with 15 commercial microbial‐enzyme products, for detergent or textile industries. Enzymes expressed in chloroplasts are functional at broad pH/temperature ranges as crude‐leaf extracts, while most purified commercial enzymes showed significant loss at alkaline pH or higher temperature, required for broad range commercial applications. In contrast to commercial liquid enzymes requiring cold storage/transportation, chloroplast enzymes as a leaf powder can be stored up to 16 months at ambient temperature without loss of enzyme activity. Chloroplast‐derived enzymes are stable in crude‐leaf extracts without addition of protease inhibitors. Leaf lipase/mannanase crude extracts removed chocolate or mustard oil stains effectively at both low and high temperatures. Moreover, leaf lipase or mannanase crude‐extracts removed stain more efficiently at 70 °C than commercial microbial enzymes (<10% activity). Endoglucanase and exoglucanase in crude leaf extracts removed dye efficiently from denim surface and depilled knitted fabric by removal of horizontal fibre strands. Due to an increased demand for enzymes in the food industry, marker‐free lettuce plants expressing lipase or cellobiohydrolase were created for the first time and site‐specific transgene integration/homoplasmy was confirmed by Southern blots. Thus, leaf‐production platform offers a novel low‐cost approach by the elimination of fermentation, purification, concentration, formulation and cold‐chain storage/transportation. This is the first report of commercially launched protein products made in leaves and validated with current commercial products. [ABSTRACT FROM AUTHOR]

Fragrance allergy is a lifelong condition, and the probability of being affected increases with frequent exposure to fragrance. Currently, fragrance-free laundry detergents are not common in supermarkets. We used a contingent valuation among Austrian consumers in a within-respondent treatment to estimate how willingness to pay is influenced by health information. We found that higher income groups have a higher willingness to pay for fragrance-free detergents. Informing consumers about health impacts substantially increases this difference. Our simulation shows that lower-income groups benefit from health information only if low-priced fragrance-free detergents are available on the market. [ABSTRACT FROM AUTHOR]

Defects in the epithelial barrier have recently been associated with asthma and other allergies. The influence of laundry detergents on human bronchial epithelial cells (HBECs) and their barrier function remain unknown. We investigated the effects of laundry detergents on cytotoxicity, barrier function, the transcriptome, and the epigenome in HBECs. Air-liquid interface cultures of primary HBECs from healthy control subjects, patients with asthma, and patients with chronic obstructive pulmonary disease were exposed to laundry detergents and detergent residue after rinsing. Cytotoxicity and epithelial barrier function were evaluated. RNA sequencing, Assay for Transposase Accessible Chromatin with high-throughput sequencing, and DNA methylation arrays were used for checking the transcriptome and epigenome. Laundry detergents and rinse residue showed dose-dependent toxic effects on HBECs, with irregular cell shape and leakage of lactate dehydrogenase after 24 hours of exposure. A disrupted epithelial barrier function was found with decreased transepithelial electrical resistance, increased paracellular flux, and stratified tight junction (TJ) immunostaining in HBECs exposed to laundry detergent at 1:25,000 dilutions or rinse residue at further 1:10 dilutions. RNA sequencing analysis showed that lipid metabolism, apoptosis progress, and epithelially derived alarmin-related gene expression were upregulated, whereas cell adhesion–related gene expression was downregulated by laundry detergent at 1:50,000 dilutions after 24 hours of exposure without substantially affecting chromatin accessibility and DNA methylation. Our data demonstrate that laundry detergents, even at a very high dilution, and rinse residue show significant cell-toxic and directly disruptive effects on the TJ barrier integrity of HBECs without affecting the epigenome and TJ gene expression. [ABSTRACT FROM AUTHOR]

Cellulases, lipases, proteases, and amylases are employed in the detergent preparation to speed up the detergency process. Microbial cellulases are now commercially manufactured and are being used by various industries like detergent industry. Currently, the supplementation of detergent‐compatible enzymes is a new trend followed by most of the detergent industries. The cellulases are supplemented to the detergents to improve the fabric smoothness and soil removal without damaging them. They act by passing through the textile interfibril spaces and thus the fabric quality is preserved. The process is environment friendly, and the use of cellulases and other detergent‐compatible enzymes diminishes the utilization of toxic detergent constituents that are hazardous to humans. Alkaline cellulases active at ambient and low temperature are now preferred to maintain the fabric quality and use of low energy. The review reports on the production, purification, and properties studies of detergent‐compatible proteases, amylases, and lipases are available. However, there is no report on detergent‐compatible bacterial cellulases. In the present review, an overview on the production, purification, and characterization of detergent bacterial cellulases is presented. The stability and compatibility of the alkaline bacterial cellulases in the presence of the detergents and the detergent constituents are also discussed. [ABSTRACT FROM AUTHOR]

Abstract The detergent-compatible alkaline protease was produced from the bacterial strain Bacillus sp. APP-07 isolated from Laundromat soil of Solapur, Maharashtra, India. The culture was grown in 1000 ml capacity baffled flask with a working volume of 100 ml and incubated at 55 °C for 33 h on a rotary shaker. After incubation, alkaline protease was partially purified by the sequential method of acetone precipitation followed by nominal molecular weight limit (NMWL) cut-off ultrafiltration using 50 K and 10 K filters. Finally, Sephadex G-100 gel filtration chromatographic purification was performed to obtain 3.12 fold purified alkaline protease enzyme with a 66.67% final yield. The purified enzyme showed 31907.269 units (U) of enzyme activity containing 8741.718 U/mg of specific enzyme activity. The molecular weight of the enzyme was confirmed about 33.0 kDa (kDa) by the SDS-PAGE analysis. The purified enzyme was stable at higher pH and temperature range, with an optimum pH 10.5 and temperature 55 °C. The enzyme showed excellent stability and compatibility in various detergents, surfactants, bleach, and oxidizing agents. The enzyme activity enhanced in the presence of Ca2+, Cu2+, and surfactants, whereas; the phenylmethylsulphonyl fluoride (PMSF) and Diisopropyl fluorophosphate (DFP) completely inhibit the enzymatic activity, which pointed out that the enzyme affiliated to serine-centered metalloproteases family. In conclusion, the remarkable tolerance and stability of the enzyme explored the promising candidature for the several potential applications in the laundry detergents. The sustainability of the enzyme might serve several possible applications in the laundry detergents, leather industries, and other harsh industrial processes. [ABSTRACT FROM AUTHOR]

Liquid protease was added to the preferred basic formula. The cold and heat resistance of different detergents were evaluated and the detergency upon the protein-stained cloth was observed. The effects of different conditions on the detergency of detergents were studied.The results showed that the three detergents as prepared had good stability. The detergent added with protease was significantly improved in the detergency to protein-stained cloth, and the detergency powers were increased by 45.1% and 33.3%, respectively, for two types of proteases. The optimum washing conditions for the enzymatic detergent were as follows: temperature of 25-35 C soaking time of 10-20 min, and washing time of 5-10 min. Washing by hand or by machine could be chosen according to actual situation. [ABSTRACT FROM AUTHOR]

Oral lichenoid lesions (OLLs) are a diverse group of disorders that may be attributed to an autoimmune etiology, underlying systemic disease, or in association with an identifiable causative agent, such as a medication, food product, or dental material. OLLs commonly present with striae, erythema, and/or ulceration on affected oral mucosa and can be symptomatic. The aim of this report is to describe a case of OLLs that were believed to be attributed to use of household laundry detergent to clean an oral occlusal appliance. [ABSTRACT FROM AUTHOR]

Background: European legislation has banned the preservative methylisothiazolinone (MI) from inclusion in leaveon cosmetics. However, the risk for allergic reactions depends on exposure. The aim of this study was to determine the risk of MI in laundry detergents for household machine washing. Methods: Different formulations of laundry detergents with commercial MI levels, up to one thousand ppm were used and three different types of clothes were washed in a normal household machine setting one time and 10 times. The level of MI was measured by HPLC. Results: While MI could be retrieved in the positive control of clothes drenched with washing powder but not washed afterwards, MI could not be detected in any specimen of clothes washed under household conditions. The detection limit was 0.5 ppm. Conclusion: It is important to discuss the difference of risk and hazard. While MI clearly is a high hazard as a strong contact allergen, the risk depends on exposure. Regarding the risk of exposure levels for the consumer to MI in clothes it can be stated that the use of MI in laundry detergents is safe for the consumer if these products are used according to the instructions in the normal household setting machine wash. [ABSTRACT FROM AUTHOR]