• Journal of Microbiology and Biotechnology
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• 제33권5호
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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.

• 한국식품영양학회지
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• 제29권5호
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• pp.760-766
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• 2016

To increase the collagen recovery rate, bromelain (PB) and a microbial enzyme (PM) were used to treat to pork skin with single agent or combinations. The quality of collagen from the pork skin was evaluated by enzymatic treatments. The highest results for the solid contents and pork skin recovery rate obtained with the microbial-enzyme-bromelain mixtue (PMB) were 13.60% and 18.05% respectively. The result also showed that the color was affected by different types of enzyme treatments. Although PM treatment showed the highest result in the protein content of 251.30 mg/100 g, PMB treatment was the highest in the test of collagen content of 37.73 g/100 g among the treatments. However bands of the pork skin were detected widely at 130 kDa and 170 kDa ranges in SDS-PAGE. The band of PB treatment showed at the range of below 17 kDa, changed into a smaller molecular weight. The collagen content test of the pork skin by the treatments, collagen contents with combination treatment of pork skin with PMB (0.5%) resulted the highest in 43.76 g/100 g. Also the fat content at the above treatment was reduced to 11.12% compared to the other treatments. With these results of this experiment, we conclude that the enzymatic treatments were effective for the processing property of pork skin like enhancing the yield of collagen.

• 한국식품과학회지
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• 제53권6호
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• pp.695-700
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• 2021

본 연구에서는 단백질 가수분해효소 0.1%와 1% Protamex를 사용하여 저분자 콜라겐을 제조하였다. 토종 닭발의 조단백질과 콜라겐의 함량은 일반 육계에 비해 높은 함량이 나타났다. 단백질 가수분해 효소농도와 반응시간이 증가할수록 낮은 분자량의 콜라겐을 얻을 수 있는 것으로 나타났다. 특히 1% Protamex로 7시간 처리한 시료가 1,000-5,000 Da의 저분자 콜라겐 함량이 55.6%로 나타났으며, 평균 분자량은 5,390 Da로 가장 낮은 분자량이 나타났다. 이는 단백질 가수분해효소 Protamex가 고분자 펩타이드 결합을 저분자 펩타이드로 분해했기 때문이다. 효소처리 콜라겐의 조직감은 고분자 펩타이드의 콜라겐이 저분자 펩타이드로 분해되어 gel을 형성하지 못하고 sol의 형태를 유지하였다. 효소농도와 효소반응시간이 증가할수록 콜라겐의 평균분자량은 작아지나 효소반응 5시간부터 평균분자량의 감소가 미미해지는 경향이 나타났다. 따라서 저분자 콜라겐 효소반응시간은 경제적으로 볼 때 5시간에서 7시간 사이가 적합하다고 할 수 있다. 이 연구결과는 향후 산업적 효소를 이용한 저분자 콜라겐 제조 및 식품 소재 활용의 기초자료로 이용할 수 있을 것이다.

• 한국식품영양과학회지
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• 제26권3호
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• pp.475-479
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• 1997

A decrease in the circulating levels of estrogen, occuring as a consequence of post menopausal decline or from surgical ovariectomy, results in an accelerated loss of bone. Estrogen has been shown to stimulate lysyl oxidase activity, and the treatment with estrogen increased the pyridinium content of cortical bone. a trivalent mature cross-links collagen fibrils named pyridinoline, which is especially abundant in collagen of cartilage and bone, markedly increases with growth in humans and rats. The main aim of this study was to examine the increased bone loss caused by ovariectomy through monitoring the concentrations of the collagen and the pyridinium cross-links of collagen, pyridinoline. The ovariectomized rats, 4 weeks old, were divided at random into two or three groups of 5. Ovariectomies were carried out on both of the saline-treated group(OVX(NH)) and the estrogen-treated group(OVX(H)) using the dorsal approach and sham operations were performed on the sham-operated group(sham). They were maintained under identical conditions for 4 or 8 weeks and were allowed free access to food and water. it was observed that there was no significant difference between the control group and the sham-operated group, however, the control group had a higher content of collagen than the saline-treated group after 4 weeks and 8 weeks. Based on these results, iot is supposed that estrogen can enhance collagen synthesis and affects the pyridinoline formation in collagen fibrils through stimulating lysyl oxidase activity.

• 한국응용과학기술학회지
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• 제30권3호
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• pp.560-566
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• 2013

In this research we extracted water-soluble collagen peptide from flatfish skin and compared it with commercially available collagen peptide extracted from Tilapia scale currently placed on the market in the aspect of physiochemical property. The physical property and nutritional components of FSCP appeared almost similarly to those of TSCP, and also in calorie, FSCP marking 3.82 Kcal showed no differences from TSCP marking 3.84 Kcal. As for forming amino acids, in aspartic acid, serine, histidine, tyrosine, methionine, FSCP had higher content than TSCP, but in OH-proline, proline and alanine FSCP had lower content than TSCP. Especially the content of essential amino acids of FSCP marked 22.74% with a higher content compared with 13.64% of TSCP. In the distribution of molecular weight FSCP with 1,000 Da showed comparatively low compared with TSCP, and in emulsion property and stability FSCP and TSCP showed similar excellent trend.

• Asian-Australasian Journal of Animal Sciences
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• 제8권6호
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• pp.577-582
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• 1995

Sixty ram lambs, weighting 23.5 kg, were randomly assigned in a $2{\times}3$ factorial arrangement of two dietary energy (high; 11.7 and low; 9.0 MJ ME/kg DM) and three levels of poultry offal meal supplementation (0, 5 and 10%). Lambs were fed ad libitum for 120-day before slaughter. At slaughter, half the lambs in each dietary treatment group were randomly selected for electrical stimulation of their undressed carcasses. The M. Biceps femoris pH and temperatures were monitored at 1, 3, 5, 8 and 24 h postmortem. At 24 h postmortem, the M. biceps femoris was removed from the fight side of each carcass and steaks were obtained for determination of Warner-Bratzler shear force, collagen content and collagen solubility. The results showed that temperature and pH values during the 24-h postmortem were consistently higher (p < .01) and lover (p < .01), respectively, for M. biceps femoris from lambs fed high energy diets than for those fed on low energy diets. Muscles from high energy fed lambs had lower (p < .01) shear force values and higher (p < .01) percent soluble collagen than for low energy fed lambs; total collagen content was not significantly influenced by dietary energy level. Increased the level of poultry offal meal supplementation in the diet to 10% was associated with concomitant increases (p < .01) in muscle tenderness and percent soluble collagen. Electrical stimulation (ES) of carcasses resulted in a lower shear force values for the M. biceps femoris than in non-stimulated carcasses (Non-ES); total collagen content and percent soluble collagen were not significantly affected by ES treatment.

• Korea-Australia Rheology Journal
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• 제19권2호
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• pp.81-88
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• 2007

Blends of collagen dispersion (COL) with poly(vinyl alcohol) (PVA) in different weight ratios were investigated by oscillatory rheometry, Fourier transform-infrared spectroscopy and scanning electron microscopy. It was found that even with 80% of PVA, the COL/PVA blends behaved more like collagen dispersion than pure PVA solution in the dynamic thermal and frequency processing, for instance, a dominant elastic appearance (G'>G"), a similar shear thinning behavior and the thermal denaturation below $40^{\circ}C$. However, influence on the blend behaviour by PVA was noticeable, for instance, an increase of dynamic denaturation temperature, the decreasing intensity of amide I, II and III bands as well as the diminishing irregular pores on the surface of blends. The interaction between collagen and PVA could be observed, especially at the regions with low content or high content of PVA.

• 한국염색가공학회지
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• 제33권3호
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• pp.131-140
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• 2021

Collagen and chitosan are used in medical and cosmetic materials as natural polymers. In order to utilize the advantages of the materials, collagen/chitosan conjugated wet-spun fibers were prepared. The analysis of surface, optical, thermal and mechanical properties was carried out on the various composition of collagen and chitosan. As a result of images analysis, it was verified that the collagen/chitosan conjugated fibers were stably spun. In addition, the optical and thermal properties of fibers were observed to be changed by hydrogen bond. As a result, an optimized composition could be found at an appropriate content. Moreover, the optimized fibers have mechanical properties similar to chitosan fibers, while improving the structural and thermal stability by its hydrogen bond. In addition, the wet-spun collagen/chitosan conjugated fibers can be applied to medical and various fields through mechanical properties according to content control.

• 한국축산식품학회지
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• 제37권3호
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• pp.392-401
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• 2017

Variations in physical toughness between muscles and animals are a function of growth rate and extend of collagen type I and III. The current study was designed to investigate the ability of growth rate, collagen concentration, collagen synthesizing and degrading genes on two different fibroblast cells derived from Hanwoo m. longissimus dorsi (LD) and semimembranosus (SM) muscles. Fibroblast cell survival time was determined for understanding about the characteristics of proliferation rate between the two fibroblasts. We examined the collagen concentration and protein expression of collagen type I and III between the two fibroblasts. The mRNA expression of collagen synthesis and collagen degrading genes to elucidate the molecular mechanisms on toughness and tenderness through collagen production between the two fibroblast cells. From our results the growth rate, collagen content and protein expression of collagen type I and III were significantly higher in SM than LD muscle fibroblast. The mRNA expressions of collagen synthesized genes were increased whereas the collagen degrading genes were decreased in SM than LD muscle. Results from confocal microscopical investigation showed increased fluorescence of collagen type I and III appearing stronger in SM than LD muscle fibroblast. These results implied that the locomotion muscle had higher fibroblast growth rate, leads to produce more collagen, and cause tougher than positional muscle. This in vitro study mirrored that background toughness of various muscles in live animal is likely associated with fibroblast growth pattern, collagen synthesis and its gene expression.

• 한국축산식품학회지
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• 제34권6호
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• pp.727-735
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• 2014

This study was conducted to determine the effects of using mechanically deboned chicken meat (MDCM) and collagen on quality characteristics of semi-dried chicken jerky. In experiment I, semi-dried chicken jerky was prepared with the replacement of chicken breast with MDCM (0, 10, 20, and 30%). The pH value of the jerky formulated with only chicken breast was 5.94, while the replacement of chicken breast with MDCM significantly increased the pH (p<0.05). The protein content and shear force of the jerkies decreased with increasing amounts of MDCM, whereas the fat, ash content and processing yield showed the opposite tendency (p<0.05). Replacement with up to 10% MDCM had no adverse effects on the sensory characteristics of the semi-dried chicken jerky. In experiment II, four levels of pork collagen (0, 1, 2, and 3%) were added to the semi-dried chicken jerky formulated with 90% chicken breast and 10% MDCM. The addition of collagen increased the moisture content, but decreased the ash content of the jerkies produced (p<0.05). The processing yield of the jerkies increased with increasing added amounts of collagen (p<0.05). It was found that the jerkies formulated with 0-2% collagen had significantly higher overall acceptance score than those prepared with 3% collagen (p<0.05). In conclusion, MDCM and collagen could be useful ingredients to reduce the production cost and improve the processing yield of semidried chicken jerky. The optimal levels of MDCM and collagen which could be added without adverse effects on the sensory characteristics were up to 10% and 2%, respectively.