生物医学材料胶原蛋白的研究进展(Ⅰ)——胶原的分离纯化及交联

胶原现已被视为最有用途的生物材料。胶原所具有的优越的生物相容性和安全性、生物可降解性和弱抗原性,使得它已成为医学应用中最基本的材料。主要介绍了生物医学材料胶原蛋白的最新研究进展。首先介绍的是胶原的分离纯化及交联。     

生物医学材料胶原蛋白的研究进展(Ⅱ)-胶原的性质及其在生物医学领域的应用

胶原现已被视为最有用途的生物材料.胶原所具有的优越的生物相容性和安全性、生物可降解性和弱抗原性,使得它已成为医学应用中最基本的材料.主要介绍了生物医学材料胶原蛋白的最新研究进展.     

生物医学材料胶原蛋白的研究进展(I)-胶原的分离纯化及交联

胶原现已被视为最有用途的生物材料.胶原所具有的优越的生物相容性和安全性、生物可降解性和弱抗原性,使得它已成为医学应用中最基本的材料.主要介绍了生物医学材料胶原蛋白的最新研究进展.首先介绍的是胶原的分离纯化及交联.     

胶原水解产物生物功能性的研究进展

胶原是动物体内含量最丰富的蛋白质,其特有的三股螺旋结构以及氨基酸序列使得胶原及其水解产物具有生物相容性、生物功能性等诸多优点,可以广泛地应用于生物医学、组织工程、食品保健等领域。本文结合国内外最新研究成果,综述了胶原水解产物的生物功能性,包括抗菌性能、抗氧化性和降血压等。指出我国胶原相关产业的发展除了生产传统的组织工程和医药材料之外,还应该根据其特性,拓展其应用范围,开发出各种具有生物功能性的食品和保健品。     

专利技术

正专利名称:用于制备含有胶原原纤维的生物制造材料的方法专利公开号:CN107429479A申请人:现代牧场股份有限公司摘要:描述了一种用于从胶原或胶原样蛋白质中生产生物制造材料的方法。所述胶原或胶原样蛋白质从动物来源中分离或通过重组DNA技术或通过化学合成生产。通过胶原或胶原样蛋白质被原纤化、交联、脱水和润滑,因而形成具有基本上均匀的胶原原纤维网络的所述生物制造材料。     

胶原在止血材料中的应用

胶原具有如高拉伸强度、生物相容性和低细胞毒性以及促进细胞增殖分化等特点,是一种具有良好性能的生物材料,作为生物止血材料一直是国内外研究的热点。本文以胶原止血材料的物理形态分类,分析了几类常见形态的胶原止血材料的制备及在动物、临床试验的应用评价,并展望了未来胶原止血材料的发展趋势。     

专利文摘

正【名称】含有胶原原纤维的生物制造材料【公开号】107429066A【申请人】现代牧场股份有限公司【摘要】公开了一种含有交联胶原原纤维网络的生物制造材料。此材料主要由同样是天然皮革的主要组分的胶原组成,并且通过将胶原分子原纤化成原纤维、交联所述原纤维并且润滑所述交联的原纤维的方法来产生。与天然皮革不同,这种生物制造材料表现出非各向异性(并非方向依赖性)物理性质,例如生物制造材料片在不同方向上伸展或施加     

生物敷料的现状及展望

生物敷料在治疗烧创伤引起的皮肤组织缺损中已得到广泛应用.本文将生物敷料分为胶原类敷料和非胶原类敷料,并分别综述了其研究现状.胶原类敷料种类繁多,其中猪皮敷料来源广、价格低、使用方便;纯胶原敷料较前者抗原性低,但其降解速率过快,且机械性能差;复合型胶原膜敷料在机械性能方面优于纯胶原敷料.壳聚糖、藻酸盐等制备的非胶原类敷料虽具有一定的止血作用和生物活性,但其细胞相容性和表面活性不如胶原类材料.目前生物敷料还没有达到理想的要求,今后应重点利用纳米技术和组织工程技术,开发纳米生物敷料和组织工程化敷料.     

胶原生物材料在临床医学上的应用

简述胶原生物医用材料的作用、优势,在临床医学上的广泛应用和发展前景。     

胶原蛋白及其用于组织工程的最新研究

胶原蛋白是一组多糖蛋白分子的大家族,现在已被发现的有27种。胶原特殊的螺旋结构赋予它许多优良的性质:低免疫性、生物相容性、可生物降解性、止血性和促进细胞生长。目前．生物可降解的胶原材料是组织工程中研究较多的一类材料,广泛应用于皮肤替代物、骨组织工程和其他生物组织工程。对胶原蛋白的性质及其在组织工程领域的最新研究进行了综述。     

Age of Farmed Atlantic Salmon at Seawater Transfer Affects Muscle Collagen Content and Solubility at Harvest

Salmon released to seawater as different smolt types differed significantly in the total collagen content and the solubility of the collagen present. A 11/2 smolt contained more total collagen than 1/2 and 1 smolt types. Less insoluble collagen and more of the pepsin soluble collagen was generally present in 11/2 smolt type as compared with both 1/2 and 1 types, with the exception of prerigor type 1 salmon. No differences between smolt types in acetic soluble collagen were present. Fish with the higher amount of collagen also had the lowest end pH. Although the bled body weight differed, no correlation between body weight and collagen content or its solubility was found. Fish with higher end pH had lower total collagen and pepsin soluble collagen (r = ‐0.77, P = 0.0001 and r = ‐0.51, P = 0.04, respectively, and more insoluble collagen (r = 0.72, P = 0.002).     

胶原的生物合成过程及其调节

胶原的生物合成涉及一系列的复杂过程,主要包括胶原基因的转录、翻译、胶原分子的后加工、分泌及聚 集等。本文介绍了胶原的生物合成过程,生物合成中所涉及的酶,胶原分子的结构,聚集态结构,调节胶 原合成的多种因素,并对已确定的１８种胶原类型,３２种具有遗传特异性的多肽链以及它们在动物体内 的分布作了简要描述。     

COLLAGEN AS A HAMBURGER EXTENDER

Bovine hide collagen was added to ground beef at 0, 10 or 20% level replacing lean meat and stored at ?15°C up to 2 weeks to evaluate the effect of collagen level and storage time on the quality. Beef patties with collagen were found to be superior (P<0.05) in juiciness by the taste panel while the flavor, texture and overall acceptability decreased as the collagen level increased. However, no significant differences were observed for these attributes due to storage time. Collagen was found to bind moisture as indicated by no significant cooking loss due to replacement levels or storage. Chemical rancidity decreased significantly as the collagen level increased but was not influenced by length of storage. The addition of collagen to ground beef resulted in a lighter colored patty which was influenced by collagen level and storage time. The patties tended to become less cohesive as collagen level increased but the texture improved upon storage.     

胶原凝胶性质影响因素的研究进展

为解决畜禽及鱼类副产物利用率不高以及胶原凝胶类食品品类单一的问题,本文介绍胶原的概念、来源和结构,简述胶原的凝胶性质,综述胶原浓度、胶原溶液pH值、加热温度等环境因素对胶原凝胶性质的影响和γ-聚谷氨酸、卡拉胶、天然植物多元酚、醇类、盐、谷氨酰胺转氨酶和聚丙烯酸钠7 种添加物对胶原凝胶性质改良的研究进展,指出目前胶原凝胶研究的不足之处和未来研究的可能方向,旨在为利用此类副产物进行胶原凝胶类食品研发以及更好地将胶原凝胶应用于食品工业等领域提供思路和依据。     

酶解技术提取动物组织中的胶原蛋白及其肽的研究进展

胶原蛋白是哺乳动物各组织器官中含量最丰富、覆盖面最广,与生物体组织和器官功能息息相关的蛋白质,胶原蛋白经蛋白酶水解可形成胶原蛋白肽。本文综述了酶提胶原蛋白的原材料、所用酶的种类、相关酶提辅助技术和产物性质的检测方法,从而为胶原蛋白及胶原蛋白肽提取工艺的优化和应用市场的扩展提供理论依据。     

添加鱼皮胶原蛋白蛋黄酱加工工艺的研究

通过正交试验确定鱼皮胶原蛋白作为乳化剂在蛋黄酱生产中加入的最佳配方,配方为鱼皮胶原蛋白2%,蛋黄15%,醋酸0.3%.水10%.结果表明,鱼皮胶原蛋白代替部分蛋黄,起到一定的乳化效果,同时还能增加蛋白质的含量.鱼皮胶原蛋白舍有多种氨基酸,易于消化吸收,一直受到食品领域的关注,而且胶原蛋白作为一种蛋白质,还具有各种生理功...     

鱼皮胶原蛋白在蛋黄酱加工应用中的初步研究

通过正交实验确定了鱼皮胶原蛋白作为乳化剂在蛋黄酱生产中加入的最佳配方,配方为鱼皮胶原蛋白3%,蛋黄15%,醋酸0.3%,水10%。研究结果表明,鱼皮胶原蛋白代替部分蛋黄,起到一定的乳化效果,同时还能增加蛋白质的含量。     

Albumin production activity of primary rat hepatocytes is improved on type V collagen

Primary rat hepatocytes were cultured on type V collagen. Hepatocyte spreading on type V collagen was inferior compared with that on type I collagen. However, the albumin production rates of hepatocytes cultured on type V collagen were approximately twice as high as those of hepatocytes cultured on type I collagen.     

Exploration of collagen recovered from animal by-products as a precursor of bioactive peptides: Successes and challenges

A large amount of food-grade animal by-products is annually produced during industrial processing and they are normally utilized as animal feed or other low-value purposes. These by-products are good sources of valuable proteins, including collagen or gelatin. The revalorization of collagen may lead to development of a high benefit-to-cost ratio. In this review, the major approaches for generation of collagen peptides with a wide variety of bioactivities were summarized, including antihypertensive, antioxidant and antidiabetic activities, and beneficial effects on bone, joint and skin health. The biological potentials of collagen peptides and their bioavailability were reviewed. Moreover, the unique advantages of collagen peptides over other therapeutic peptides were highlighted. In addition, the current challenges for development of collagen peptides as functional food ingredients were also discussed. This article discusses the opportunity to utilize collagen peptides as high value-added bio-functional ingredients in the food industry.     

Isolation and partial characterization of pepsin-soluble collagen from the skin of grass carp (Ctenopharyngodon idella)

Pepsin-soluble collagen was extracted from the skin of grass carp (Ctenopharyngodon idella) with a yield of 46.6%, on a dry weight basis. Electrophoretic patterns showed that the collagen contained α1 and α2 chains, similar to those of calf skin collagen. The imino acid content of the collagen from grass carp skin was much lower than those of mammalian’s collagens, as also were the transition temperature and denaturation temperature which were only 24.6 °C and 28.4 °C respectively. Peptide maps of the collagen digested by trypsin and V8 protease showed different peptide fragments from those of calf skin collagen and other fish skin collagens, suggesting differences in amino acid sequences and collagen conformation. In addition, the lyophilized collagen sponge from grass carp skin had a uniform and regular network structure, just like calf skin collagen sponge. These results suggest that grass carp skin has potential for use as a supplementary source of collagen.