• Journal of the Society of Cosmetic Scientists of Korea
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• v.48 no.4
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• pp.385-392
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• 2022

In this study, keratin peptides were produced through high-temperature anaerobic fermentation of keratin, a protein contained in deer antler, with Fervidobacterium islandicum AW-1, and factors related to human hair, confirming the possibility of keratin peptides as cosmetic ingredients. As a result of the cytotoxicity and proliferation of deer antler fermented keratin peptide according to the concentration in the dermal papilla cell line, cytotoxicity was not observed and the cell proliferation effect was shown. For human dermal papilla cells, statistically significant increasing in growth factors according to the deer antler fermented keratin peptide was determined possiblity of effects on hair growth. Cosmetic products containing deer antler fermented keratin peptides were manufactured and skin safety and anti hair loss efficacy clinical tests were conducted. As a result, after 12 weeks of use, the total number of hairs statistically significant increased compared to before using the product and the difference in total number of hairs compared to the control group was found. In conclusion, we suggest that the possibility of fermented deer antler keratin peptide as a cosmeceutical ingredient as well as a health functional food material was confirmed.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.46 no.3
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• pp.243-252
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• 2020

Using Fervidobacterium islandicum AW-1, polar low molecular weight keratin peptides were produced and confirmed through factors related to the skin elasticity. As a result of confirming the cytotoxicity and collagen synthesis ability according to the concentration of the polar low molecular weight keratin peptide in human fibroblasts, it was confirmed that the cytotoxicity did not appear and the collagen synthesis in human fibroblasts was increased. A mask pack containing a polar low-molecular weight keratin peptide was used, and a test product was used for 4 weeks in 22 healthy women subjects. As a result, it showed statistically significant effects on skin elasticity, skin torsion elasticity, skin color and moisture improvement. Through this test, it was confirmed that the polar low-molecular keratin peptide can be used as a cosmetic ingredient that helps improve skin elasticity.

• Advances in environmental research
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• v.11 no.1
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• pp.1-16
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• 2022

Amongst 27 isolates from deteriorated leather samples, Arthrobacter creatinolyticus KP015744 zzx28 was found to be an efficient collagenase producer. Collagenase production of 13.33 µmoles/min was shown at an optimum temperature at 37℃ after 72h and at pH 7.5 by using 2 ml/dL inoculum in 10 mg/ml collagen peptide type I as a substrate. In presence of Hg²⁺, EDTA and 𝛽-mercaptoethanol the collagenase production by the isolate was strongly inhibited however Fe²⁺, Ca²⁺and DMSO enhanced production of the enzyme. Specific activity was found to be 19.46×10³ U/mg and molecular weight 66 kD by SDS PAGE. Isolate also has potential to hydrolyze keratin which is another important protein found in leather. Experimental results propose that collagenase can be effectively used as a tool for collagen and keratin rich solid waste treatment.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.45 no.4
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• pp.353-361
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• 2019

Using Fervidobacterium islandicum AW-1, keratin peptides were produced and confirmed factors related to the scalp and hair. The cytotoxicity and proliferation tests as a function of the concentration of the keratin peptide did not show toxicity and effect on the cellular proliferation in the immortalized human hair dermal papilla cell line. Hair shampoos and hair essences containing keratin peptides were produced, and conducted human patch test. Result showed no skin irritation. The shampoo and the essence were apploed to 2 groups of 30 healthy adults for 4 weeks and showed statistically significant positive results for gloss, hair loss, scalp trouble, and hair roughness by visual assessment. The scalp water content was significantly increased after 2 and 4 weeks compared to before using the shampoo or the essence. Trans-epidermal water loss (TEWL) and the sebum secretion amount in the scalp were significantly decreased after 4 weeks compared to before. The frictional force against combing before and after using the hair shampoo and the essence for normal hair tress and damaged hair tress was significantly changed. The combing force was increased for normal hair tress and decreased for damaged hair tress. In conclusion, we suggest that keratin peptides are appropriated as cosmetic ingredients to be used in hair and scalp related products.

• Journal of People, Plants, and Environment
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• v.22 no.1
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• pp.39-52
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• 2019

To evaluate the protective effect of collagen peptide-coated coffee extract on skin aging, cell viability was measured with a MTT assay using cultured CCD-986sk fibroblasts, and its effect on wrinkles in the skin of hairless mice induced by UVB-irradiation was examined. In addition, its effect on procollagen synthesis and anti-oxidative, and its inhibitory activity against collagenase, elastase, tyrosinase and MMP-1 were analysed. After the 30-minute topical treatment, the animals were exposed to UVB irradiation (60-100 mJ/cm²) for 4 weeks and its intensity increased during the period. Under the experimental conditions set in this study, the skin thickness of hairless mice significantly decreased (11.8-21.3%) compared to the control group. Based on these results, the prolonged oral intake of a collagen peptide mixture with coffee is expected to significantly increase the synthesis of procollagen in dermal fibroblasts, thereby contributing to the alleviation of wrinkling and lowered elasticity due to structural damage to the dermal layer caused by UV. The oral intake of collagen-coated coffee contributes to increasing collagen biosynthesis in a dose-dependent manner and alleviates the symptoms of thickened keratin caused by UV irradiation. However, it did not inhibit the enzymes involved in skin aging, whitening, wrinkle improvement, and antioxidation. Based on the these results, it can be concluded that the intake of collagen peptide-coated coffee extract can be utilized as an alternative material for the prevention or treatment of diseases associated with photoaging.

• Journal of Dairy Science and Biotechnology
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• v.34 no.1
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• pp.1-7
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• 2016

Colostrum, a nutrient-rich fluid produced by female mammals after giving birth, is the specific initial diet of mammalian neonates. Colostrum is important for the nutrition, growth, and development of newborn infants and contributes to the immunologic defense of neonates. It contains immunoglobulins, antimicrobial peptides, such as lactoferrin and lactoperoxidase, and other bioactive molecules, including growth factors, such as IGF (insulin-like growth factor), EGF (epithermal growth factor), $TGF-{\beta}$ (transforming growth factor), and FGF (fibroblast growth factor). Bovine colostrum is a rich source of growth factors, which play a central role in wound healing. The biological activities of colostrum emphasize the relevance of the synergistic activity of growth factors to stimulate keratinocyte proliferation and migration, which are essential for tissue repair. Colostrum increases the expression of early differentiation markers, such as keratin 1 and 10 and involucrin, and late differentiation markers, including loricrin and filaggrin. Additionally, colostrum increases granulation tissue volume in the dermis, suggesting that it has a beneficial effect on wound healing. The therapeutic use of colostrum or individual peptides present in colostrum has a positive and curative influence on various gastrointestinal diseases.

• Microbiology and Biotechnology Letters
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• v.49 no.1
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• pp.65-74
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• 2021

Serine proteases are the most versatile proteolytic enzymes with tremendous applications in various industrial processes. This study was designed to investigate the biochemical properties, critical residues, and the catalytic potential of alkaline serine protease using in-silico approaches. The primary sequence was analyzed using ProtParam, SignalP, and Phyre2 tools to investigate biochemical properties, signal peptide, and secondary structure, respectively. The three-dimensional structure of the enzyme was modeled using the MODELLER program present in Discovery Studio followed by Molecular Dynamics simulation using GROMACS 5.0.7 package with CHARMM36m force field. The proteolytic potential was measured by performing docking with casein- and keratin-enriched residues, while the effect of the inhibitor was studied using phenylmethylsulfonyl fluoride, (PMSF) applying GOLDv5.2.2. Molecular weight, instability index, aliphatic index, and isoelectric point for serine protease were 39.53 kDa, 27.79, 82.20 and 8.91, respectively. The best model was selected based on the lowest MOLPDF score (1382.82) and DOPE score (-29984.07). The analysis using ProSA-web revealed a Z-score of -9.7, whereas 88.86% of the residues occupied the most favored region in the Ramachandran plot. Ser327, Asp138, Asn261, and Thr326 were found as critical residues involved in ligand binding and execution of biocatalysis. Our findings suggest that bioengineering of these critical residues may enhance the catalytic potential of this enzyme.