• Journal of Microbiology and Biotechnology
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• v.33 no.5
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• pp.656-661
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• 2023

The aims of this study were to optimize the preparation of low-molecular-weight collagen using a proteolytic enzyme (alcalase) derived from the feet of Korean native chickens, and to characterize the process of collagen hydrolysis. Foreign bodies from chicken feet were removed using ultrasonication at 28 kHz with 1.36 kW for more than 25 min. The hydrolytic pattern and molecular weight distribution of enzyme-treated collagen from chicken feet were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and high-performance liquid chromatography, respectively. Ideally, chicken feet should be treated at 100℃ for 8 h to obtain a high collagen content using hot water extraction. The collagen content of the chicken foot extract was 13.9 g/100 g, and the proportion of low-molecular-weight collagen increased with increasing proteolytic enzyme concentration and reaction time. When treated with 1% alcalase, the average molecular weight of collagen decreased rapidly to 4,929 Da within 5 h and thereafter decreased at a slower rate, reaching 4,916 Da after 7 h. Size exclusion chromatography revealed that low-molecular-weight collagen peptides of approximately 1,000-5,000 Da were obtained after hydrolysis with 1% alcalase for 1 h.

• Korean Journal of Food Science and Technology
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• v.53 no.6
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• pp.695-700
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• 2021

The purpose of this study was to prepare low-molecular weight collagen using a commercial proteolytic enzyme (Protamex) from collagen extracted from feet of Korean native chicken and to investigate the quality characteristics of this collagen. The collagen content of Korean native chicken feet was 13.9 g/100 g, which was higher than the 6.21 g/100 g of general broilers. It was found that the content of low molecular weight collagen increased as the concentration of proteolytic enzymes and reaction time increased. In particular, reaction with 1% Protamex for 7 h resulted in 55.6% of low molecular weight (1,000-5,000 Da) collagen content, and the average molecular weight was 5,390 Da. Regarding the texture of the enzyme-treated collagen, the collagen with high molecular weight peptides decomposed into low molecular weight peptides, and the gel type could not be formed, whereas the sol type was maintained.

• Mass Spectrometry Letters
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• v.12 no.3
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• pp.81-84
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• 2021

Collagen, which accounts for one-third of human protein, is reduced due to human aging, and much attention is focused on making collagen into food to prevent such aging. Gel permeation chromatography with Reflective Index (RI) detection (GPC/RI) was chosen as the most suitable instrument to confirm molecular weight distribution, and we explored the use of this technique for analysis of collagen peptide molecular sizes and distributions. Data reliability was verified by matrix-assisted laser desorption/ionization coupled to time-of-flight (MALDI-TOF) mass spectrometric analysis. The data were considered meaningful for comparative analysis of molecular weight distribution patterns.

• Journal of Microbiology and Biotechnology
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• v.31 no.10
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• pp.1401-1408
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• 2021

This study examined whether the oral administration of low-molecular-weight collagen peptide (LMCP) containing 3% Gly-Pro-Hyp with >15% tripeptide (Gly-X-Y) content could ameliorate osteoarthritis (OA) progression using a rabbit anterior cruciate ligament transection (ACLT) model of induced OA and chondrocytes isolated from a patient with OA. Oral LMCP administration (100 or 200 mg/kg/day) for 12 weeks ameliorated cartilage damage and reduced the loss of proteoglycan compared to the findings in the ACLT control group, resulting in dose-dependent (p < 0.05) improvements of the OARSI score in hematoxylin & eosin (H&E) and Safranin O staining. In micro-computed tomography analysis, LMCP also significantly (p < 0.05) suppressed the deterioration of the microstructure in tibial subchondral bone during OA progression. The elevation of IL-1β and IL-6 concentrations in synovial fluid following OA induction was dose-dependently (p < 0.05) reduced by LMCP treatment. Furthermore, immunohistochemistry illustrated that LMCP significantly (p < 0.05) upregulated type II collagen and downregulated matrix metalloproteinase-13 in cartilage tissue. Consistent with the in vivo results, LMCP significantly (p < 0.05) increased the mRNA expression of COL2A1 and ACAN in chondrocytes isolated from a patient with OA regardless of the conditions for IL-1β induction. These findings suggest that LMCP has potential as a therapeutic treatment for OA that stimulates cartilage regeneration.

• 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.

• Korean Journal of Materials Research
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• v.34 no.4
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• pp.215-222
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• 2024

Because collagen is inherently piezoelectric, research is being actively conducted to utilize it to harvest energy. In this study, a collagen solution was prepared using edible low-molecular-weight peptide collagen powder, and collagen films were fabricated using a dip coating method. The collagen films prepared by dip coating showed a smooth surface without defects such as pinholes or cracks. Dehydrothermal treatment of the collagen films was performed to induce a stable molecular structure through cross-linking. The collagen film subjected to dehydrothermal treatment at 110 ℃ for 24 h showed a thickness reduction rate of 19 %. Analysis of the collagen films showed that the crystallinity of the collagen film improved by about 7.9 % after dehydrothermal treatment. A collagen film-based piezoelectric nanogenerator showed output characteristics of approximately 13.7 V and 1.4 ㎂ in a pressure test of 120 N. The generator showed a maximum power density of about 2.91 mW/m² and an output voltage of about 8~19 V during various human body movements such as finger tapping. The collagen film-based piezoelectric generator showed improved output performance with improved crystallinity and piezoelectricity after dehydrothermal treatment.

• Journal of Applied Biological Chemistry
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• v.62 no.1
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• pp.101-107
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• 2019

The objectives of this study were to evaluate the anti-aging effects and investigate the effect of simulated gastrointestinal (GI) digestion on the anti-aging properties and intestinal permeation of the potential fish collagen hydrolysates (FCH). Therefore, procollagen synthesis, matrix metalloproteinase-1 (MMP-1) production, and Caco-2 cell permeability were analyzed before and after in vitro digestion for FCHs, low-molecular weight fractions (<1 kDa), and high molecular weight fractions (>1 kDa). After being subjected to GI digestion, the level of MMP-1 inhibition was maintained, although the procollagen production was significantly (>20%) lower with all samples. Also, the digested FCHs and their <1 kDa fraction yielded 9.1 and 13.8% increased peptide transport, respectively, compared to undigested samples. Based on the effective intestinal permeation and high digestive enzyme stability, the <1 kDa fraction of FCHs is a potential bioactive material suitable for anti-aging applications in the food and cosmetics industries.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.38 no.4
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• pp.321-326
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• 2012

Recent studies have revealed that collagen peptide plays a protective role on skin by improving the activity of antioxidants and acts as an inducer of skin regeneration. To evaluate the efficacy of low molecular weight collagen peptide for skin recovery after non-ablative 1550 nm fractional photothermolysis laser. 10 volunteers were randomly divided into two groups. Both control and experimental groups received fractional photothermolysis treatment. In the experimental group, 5 subjects received oral collagen peptide 1,000 mg/day for 8 weeks. Before and after the treatment, we measured elastic recovery of skin, transepidermal water loss (TEWL) and erythema index (EI) for each patients. The evaluation of clinical results showed that elastic recovery of skin is higher in the experimental group than the control group (p < 0.05). TEWL have no significancy between two groups and erythema rapidly disappeared in the experimental group. On the quartile grading scale, the mean patient satisfaction 4 weeks after the fractional photothermolysis treatment was 2.0 in experimental group and 1.2 in control group. The low molecular weight collagen peptide appears to be an effective conservative therapy for skin recovery after non-ablative 1550 nm fractional photothermolysis treatment.

• Food Science of Animal Resources
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• v.35 no.2
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• pp.156-163
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• 2015

The effects of low molecular-weight collagen peptides derived from porcine skin were investigated on the physicochemical and sensorial properties of chocolate ice cream. Collagen peptides less than 1 kDa in weight were obtained by sub-critical water hydrolysis at a temperature of $300^{\circ}C$ and a pressure of 80 bar. Ice cream was then prepared with gelatin powder and porcine skin hydrolysate (PSH) stabilizers mixed at seven different ratios (for a total of 0.5 wt%). There was no significant difference in color between the resulting ice cream mixtures. The increase in apparent viscosity and shear thinning of the ice cream was more moderate with PSH added than with gelatin. Moreover, the samples containing more than 0.2 wt% PSH had enhanced melting resistance, while the mixture with 0.2 wt% PSH had the lowest storage modulus at $-20^{\circ}C$ and the second highest loss modulus at 10℃, indicating that this combination of hydrocolloids leads to relatively softer and creamier chocolate ice cream. Among the seven types of ice creams tested, the mixture with 0.2 wt% PSH and 0.3 wt% gelatin had the best physicochemical properties. However, in sensory evaluations, the samples containing PSH had lower chocolate flavor scores and higher off-flavor scores than the sample prepared with just 0.5 wt% gelatin due to the strong off-flavor of PSH.

• Food Science of Animal Resources
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• v.33 no.4
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• pp.474-480
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• 2013

This study was performed to investigate the effects of high pressure/high temperature (HPHT) treatment on the recovery efficiency and characteristics of porcine placenta hydrolysates. The placenta hydrolysates were characterized by solubility, free amino acid contents, gel electrophoresis, gel permeation chromatography (GPC) and amino acid composition. Placenta was treated at 37.5 MPa of pressure combined with various temperatures (150, 170, and $200^{\circ}C$) or various holding times (0, 30, and 60 min at $170^{\circ}C$). Insoluble raw placenta collagen was partially solubilized (> 60% solubility) by the HPHT treatment. Free amino group content of placenta collagen was increased from 0.1 mM/g collagen to > 0.3 mM/g collagen after HPHT treatment, reflecting partial hydrolysis of collagen. The molecular weight ($M_w$) distribution showed evidence of collagen hydrolysis by shifting of $M_w$ peaks toward low molecular weight when treated temperature or holding time was increased. Alanine (Ala), glycine (Gly), hydroxyproline (Hyp), and proline (Pro) contents increased after the HPHT treatments compared to a decrease in the others. In particular, the increase in Gly was obvious, followed by Hyp and Pro, reflecting that placenta hydrolysates were mainly composed of these amino acids. However, increasing temperature or holding time hardly affected the amino acid compositions. These results indicate that the HPHT treatment is advantageous to hydrolyze collagen derived from animal by-products.