内源性半胱氨酸蛋白酶对刺参体壁胶原纤维结构的影响
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- 英文论文题名：Effects of endogenous cysteine proteinases on structures of collagen fibres from dermis of sea cucumber(Stichopus japonicus)
- 论文作者：刘玉欣 ; 刘自强 ; 马冬冬 ; 周大勇
- 英文论文作者：Liu Yuxin ; Liu Ziqiang ; Ma Dongdong ; Zhou Dayong ; School of Food Science and Technology ; Dalian Polytechnic University ; National Engineering Research Center of Seafood
- 年：2016
- 作者机构：大连工业大学食品学院;国家海洋食品工程技术研究中心;
- 论文关键词：刺参 ; 自溶 ; 胶原纤维 ; 半胱氨酸蛋白酶 ; 降解 ; 蛋白聚糖桥连结构
- 英文论文关键词：sea cucumber(stichopus japonicus) ; autolysis ; collagen fibres ; cysteine proteinases ; degradation ; interfibrillar proteoglycan bridges
- 会议召开时间：2016-11-09
- 会议录名称：中国食品科学技术学会第十三届年会论文摘要集
- 英文会议录名称：Abstracts of the 13th Annual Meeting of CIFST
- 语种：中文
- 分类号：TS254.1
- 学会代码：ZGSP
- 会议名称：中国食品科学技术学会第十三届年会
- 会议地点：中国北京
- 主办单位：中国食品科学技术学会
- 学会名称：中国食品科学技术学会
- 页数：2
- 文件大小：111k
- 原文格式：O
- 会议级别：全国
摘要
刺参(Stichopus japonicus)是一种珍贵的水产经济动物,具有较强的自溶能力,在受到外界的理化刺激后,体壁会出现松弛、粘液样变性等现象,破坏其品质,造成一定的经济损失。本文从新鲜海参体壁中提取胶原纤维作为体外模型,加入内源性半胱氨酸蛋白酶,研究其对刺参体壁胶原纤维结构的降解破坏情况。分别采用扫描电镜技术(SEM)、差示扫描量热技术(DSC)、傅里叶变换红外光谱分析(FTIR)、SDS-PAGE电泳技术和化学法来监测酶解过程,并揭示该蛋白酶对胶原纤维的降解机制。扫描电镜结果显示,内源性半胱氨酸蛋白酶通过破坏原纤维间的蛋白聚糖桥连结构使得胶原纤维部分解聚成胶原原纤维。DSC和FTIR结果表明内源性半胱氨酸蛋白酶可使纤维状胶原高级结构变得混乱。SDS-PAGE电泳和化学分析结果显示,内源性半胱氨酸蛋白酶可以使糖胺聚糖、羟脯氨酸和胶原蛋白片段从胶原纤维中释放。综上所述,内源性半胱氨酸蛋白酶可以通过降解原纤维间的蛋白聚糖桥连结构造成胶原纤维的降解破坏。
Sea cucumber(Stichopus japonicus,S.japonicus) is a kind of precious marine economic animal,and is very susceptible to external stimulus.External stimulus induces the autolysis of sea cucumber,which causes relaxtion,mucoid degeneration and tissue loss of body wall.Autolysis of sea cucumber,caused by endogenous enzymes,leads to postharvest quality deterioration of sea cucumber,consequently cause heavy economic losses.In this research,collagen fibers were prepared from the dermis of sea cucumber(S.japonicus),and the structural consequences of degradation of the collagen fibers caused by endogenous cysteine proteinases(ECP) from S.japonicus were examined by using scanning electron microscopy(SEM),differential scanning calorimetry(DSC),Fourier transform infrared spectroscopy(FTIR),sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE),and chemical analysis were used to monitor the process and reveal the mechanism of degradation of collagen fibres caused by this type of proteinase.Scanning electron microscopic images showed that ECP caused partial disaggregation of collagen fibres into collagen fibrils by disrupting interfibrillar proteoglycan bridges.Differential scanning calorimetry and Fourier transform infrared analysis revealed increased structural disorder of fibrillar collagen caused by ECP.SDS-PAGE and chemical analysis indicated that ECP can liberate glycosaminoglycan,hydroxyproline and collagen fragments from collagen fibres.Thus ECP can cause disintegration of collagen fibres by degrading interfibrillar proteoglycan bridges.
Sea cucumber(Stichopus japonicus,S.japonicus) is a kind of precious marine economic animal,and is very susceptible to external stimulus.External stimulus induces the autolysis of sea cucumber,which causes relaxtion,mucoid degeneration and tissue loss of body wall.Autolysis of sea cucumber,caused by endogenous enzymes,leads to postharvest quality deterioration of sea cucumber,consequently cause heavy economic losses.In this research,collagen fibers were prepared from the dermis of sea cucumber(S.japonicus),and the structural consequences of degradation of the collagen fibers caused by endogenous cysteine proteinases(ECP) from S.japonicus were examined by using scanning electron microscopy(SEM),differential scanning calorimetry(DSC),Fourier transform infrared spectroscopy(FTIR),sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE),and chemical analysis were used to monitor the process and reveal the mechanism of degradation of collagen fibres caused by this type of proteinase.Scanning electron microscopic images showed that ECP caused partial disaggregation of collagen fibres into collagen fibrils by disrupting interfibrillar proteoglycan bridges.Differential scanning calorimetry and Fourier transform infrared analysis revealed increased structural disorder of fibrillar collagen caused by ECP.SDS-PAGE and chemical analysis indicated that ECP can liberate glycosaminoglycan,hydroxyproline and collagen fragments from collagen fibres.Thus ECP can cause disintegration of collagen fibres by degrading interfibrillar proteoglycan bridges.
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