• 한국축산식품학회지
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• 제38권1호
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• pp.143-151
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• 2018

The effects of proteolytic enzymes (bromelain and bromelain+papain) and a ginger extract were assessed on collagen content and solubility, thermal shrinkage temperature of connective tissue, pH, cooking loss, drip loss, and Warner-Bratzler shear force (WBSF) of M. pectoralis profundus isolated from the beef brisket cut. Both proteolytic enzymes and ginger extract led to a significant increase in cooking loss and collagen solubility compared with untreated controls. On the other hand, the peak ($T_p$) thermal shrinkage temperature markedly decreased in all treatments compared with those in controls. Samples treated with bromelain, bromelain + papain, and ginger extract showed a significant decrease in WBSF by 36%, 40%, and 37%, respectively, compared with untreated controls. Our findings suggest that ginger extract are useful for post-mortem tenderization of meat containing high levels of collagen, compared to control even though, bromelain and bromelain + papain treatments have higher collagen solubility than ginger extract.

• 동의생리병리학회지
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• 제22권1호
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• pp.183-188
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• 2008

여성의 폐경에 의한 estrogen의 감소는 골다공증을 유발시킨다고 알려져 있다. 최근 새로운 식품으로 각광받고 있는 도라지 추출물을 인위적 갱년기 장애를 유발시킨 흰쥐에 투여하여 혈 중 ALP활성 변화와 골 중의 collagen의 함량 및 collagen 가교물질 pyridinoline과 deoxypyridinoline 함량 변화를 측정하여 그 효과를 검토해 보았다. 도라지 추출물을 갱년기를 유도한 흰쥐에 투여하여 혈 중 ALP활성 변화에 미치는 영향을 검토한 결과 난소절제에 의하여 ALP활성이 증가하였으나, 도라지 추출물 투여한 군에서 ALP활성이 억제되는 것을 확인할 수 있었다. 또한 난소 절제에 의해 연골의 collagen 함량이 감소되었는데, 이는 도라지 추출물을 투여함으로써 정상적인 수치로 증가하는 경향을 나타내어 도라지 추출물이 골 대사와 관련된 골 대사 질환에 유효한 효과를 나타낼 것으로 추측된다. 또한 collagen 가교물질로써 골대사의 biomaker인 pyridinoline 및 deoxypyridinoline의 골 중의 함량은 난소절제에 의해 감소하였고, 도라지 추출물 투여에 의해 증가하여 estrogen부족으로 인한 골 손실에 도라지 추출물이 유익한 효과를 가지는 것으로 보이며, 이는 도라지 중에 함유되어 있는 phytoestrogen에 의한 것으로 추측되어 앞으로 구체적인 검토가 필요한 것으로 사료된다.

• 유기물자원화
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• 제6권1호
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• pp.43-52
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• 1998

본 연구는 피혁 폐기물로부터 크롬 이온을 분리한 상태로 Collagen을 추출할 수 있는 최적 조건에 관한 것이다. Collagen 추출에 있어 온도, pH, 그리고 알칼리 용액 농도의 영향을 실험했다. 실험결과 점도측정에 의해 초기 변성온도는 $25^{\circ}C$, 완전 변성온도는 $31.5^{\circ}C$였다. Collagen 추출의 최적조건은 가용화 온도 $15^{\circ}C{\sim}20^{\circ}C$, pH 1.5, 알칼리 용액 3%였다. PH 1.5에서 크롬 이온이 거의 분리되었다. 탄닌 폐기물로부터 크롬 이온의 분리효율은 99.5% 이상이었다. 피혁 폐기물로부터 조단백질의 추출율은 89.%이었다. 추출된 조단백질내에 hydroxyprolne과 collagen의 함량은 각각 8.53%, 63.62%였다.

• 한국환경과학회지
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• 제25권4호
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• pp.579-588
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• 2016

본 연구에서는 홍어껍질에서 추출한 콜라겐 펩타이드 이화학적 특성과 비만 유발 쥐에 대한 투여 실험을 통해서 지방조직의 지질 감소효과를 조사하였으며, 홍어 껍질 콜라겐 펩타이드를 원료로 한 응용 제품 개발을 통하여 산업적 적용을 검토하였다. 일반성분 분석 결과 홍어 껍질 콜라겐 펩타이드는 대부분이 단백질로 이루어져 있는 고단백 저지방 물질이며, 분자량 측정 결과 약 1000 Da.의 저분자량이고, 아미노산 분석에서는 전형적인 콜라겐 단백질의 특성을 나타내었다. 비만 유발 쥐에 홍어 껍질 콜라겐 펩타이드를 500 mg/kg씩 18일간 경구 투여한 실험 결과에서 사료 섭취량과 음수량이 상당량 줄어 들었으며, 지방조직의 중성지방과 총 콜레스테롤 수치가 유의적으로 감소하였다. 홍어 껍질 콜라겐 펩타이드를 대량생산을 한 결과 제품의 최종 수율은 원료대비 약 17.23%로 상당히 높은 수율을 나타내었다. 이를 원료로 한 기능성 화장품 및 생활용품을 생산 및 출시하였다. 따라서 홍어 가공 부산물인 껍질을 재이용한 기능성 단백질 소재 개발을 통하여 건강기능식품과 화장품 분야에서의 기능성과 가격경쟁력을 갖춘 소재 개발에 기여 할 것으로 기대된다.

• 대한화장품학회지
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• 제39권4호
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• pp.271-279
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• 2013

립스틱의 보습력을 개선하기 위해 수용성 콜라겐(30 wt%)을 역미셀 방법으로 립스틱의 유상 내에 포접하였다. 콜라겐을 포함하는 역미셀은 외부상으로서 caprylic/capric triglyceride와 계면활성제인 polyoxyethylene(10) octylphenyl ether (Triton X-100)와 보조계면활성제로 aliphatic alcohol인 1-dodecanol을 이용하여 제조되었다. 콜라겐을 포접하는 역미셀의 형성 조건은 전기전도도와 methylene blue (MB)를 이용한 UV-vis spectrum을 통해 확인하였고, 콜라겐 포접체를 함유하는 역미셀의 립스틱에서 안정성 및 보습력은 레올로지 측정, 수분량 측정 및 아미노산 정량을 통해 확인하였다. 물과 계면활성제의 농도비인 W (water-pool), [$H_2O$]/[Triton X-100]는 10이하에서 안정한 역미셀이 형성되었다. 20 wt%의 콜라겐 포접 역미셀을 함유한 립스틱은 역미셀을 함유하지 않은 립스틱과 경도에서 큰 차이없이 안정하였으며, 수분량은 59%까지 개선되었고, 아미노산 함량은 92.7%였다.

• 한국잠사곤충학회지
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• 제43권1호
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• pp.49-52
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• 2001

The collagen growth effects in rats using B. mori fibroin sponge sheet, pure fibroin solution and chitosan sponge sheet were investigated. Histopathological inspection of the wound 12 days later showed the increse of a vascular ingrowth and the absence of inflammatory cells. Wound healing effects were accelerated in the order of Fibroin sponge sheet$\geq$Fibroin dressing solution〉Chitosan sponge sheet〉Control. The mean percentage of collagen production in rats after 12 days was 46.12$\pm$4.58% and 42.11$\pm$5.67% in fibroin sponge sheet and dressing solution-treated rats, respectively. These values were higher than the relative content in the chitosan sponge sheet and control groups, which was 23.87$\pm$3.24 and 2.42$\pm$0.32%, respectively.

• Advances in Traditional Medicine
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• 제2권2호
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• pp.94-100
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• 2002

Liver cirrhosis is characterized by hyperaccumulation of fibrous tissue components and is commonly observed in latter or terminal states of chronic hepatic diseases. In this study, the antifibrotic effects of GLM001 on liver cirrhosis were examined in bile duct ligated rats and patients with hepatic diseases. GLM001 (250 mg/kg rat weight/ day) was administrated to cirrhotic rats for 4 weeks and to humans for 14 weeks. Bile duct ligated rats significantly increased liver collagen content and biochemical markers of hepatic injury. Liver histology showed collagen fiber deposition was increased and the normal architecture was lost with large zones of necrosis being observed frequently. GLM001 administrated rats showed significantly decreased liver collagen content, and accumulation of collagen fiber in histological analysis. Patients, who were treated with GLM001, showed decreases in biochemical markers of hepatic diseases. These results demonstrate the usefulness of GLM001 as an antifibrotic agent for liver cirrhosis.

• 한국축산식품학회지
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• 제33권4호
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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.

• Journal of Animal Science and Technology
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• 제65권2호
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• pp.311-323
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• 2023

Beef consumers valued meat quality traits such as texture, tenderness, juiciness, flavor, and meat color that determining consumers' purchasing decision. Most research on meat quality has focused on marbling, a key characteristic related to meat eating quality. However, other important traits such as meat texture, tenderness, and color have not much studied in cattle. Among these traits, meat tenderness and texture of cattle are among the most important factors affecting quality evaluation of consumers. Collagen is the main component of connective tissues.It greatly affects meat tenderness. The objective of this study was to determine significant variants and candidate genes associated with collagen contents trait (total collagen) through genome-wide association studies (GWAS). Phenotypic and genomic data from 135 Hanwoo were used. The BLUPF90 family program and GRAMMAR method for GWAS were applied in this study. A total of 73 potential single nucleotide polymorphisms (SNPs) showed significant associations with collagen content. They were located in or near 108 candidate genes. TMEM135 and ME3 genes were identified to have the most significant SNPs associated with collagen contents trait. Data indicated that these genes were related to collagen. Biological processes and pathways for the prediction of biological functions of candidate genes were confirmed. We found that candidate genes were involved in positive regulation of CREB transcription factor activity and actin cytoskeleton related to tenderness and texture of beef. Three genes (CRTC3, MYO1C and MYLK4) belonging to these biological functions were related to tenderness. These results provide a basis for improving genomic characteristics of Hanwoo for the production of tender beef. Furthermore, they could be used they could be used as an index to select desired traits for consumers.

• 대한한의학회지
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• 제37권2호
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• pp.12-22
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• 2016

Objectives: The aim of this study was to confirm the dose-dependent skin moisturizing effects of dried pomegranate concentrate powder (PCP) and pomegranate concentrate solution (PCS) in ICR mice. Materials and methods: To observe the in vivo skin moisturizing effects and possible underlying mechanisms of PCP and PCS, oral PCP (100, 200, and 400 mg/kg) and PCS (1, 2, and 4 mL/kg) were administered to normal ICR mice. Changes in body weight, skin water content, and skin type I collagen and hyaluronan contents were measured. Additionally, the mRNA expression levels of hyaluronan synthase (Has) 1, 2, and 3, and collagen type I alpha (COL1A) 1 and 2 were determined in the dorsal skin of mice by real-time reverse transcription polymerase chain reaction (RT-PCR). Results: Significant and dose-dependent increases in dorsal skin water content and type I collagen and hyaluronan contents were seen in PCP and PCS-treated mice. Moreover, the mRNA levels of Has 1, 2, and 3, involved in hyaluronan synthesis, and of COL1A1 and COL1A2, involved in collagen synthesis, were significantly and dose-dependently upregulated in PCS- and PCP-treated mice. Conclusions: In this study, PCP and PCS led to favorable skin moisturizing effects as indicated by increased skin water content and the upregulation of hyaluronan and collagen synthesis enzymes in mice treated with PCS (4 mL/kg) and PCP (200 mg/kg).