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当前位置: 首页 > 文章 > 不同蛋白酶水解酪蛋白类大分子底物的规律研究 食品科学 2004,25 (3) 36-43
Position: Home > Articles > Study on Hydrolysis Conditions of Macromolecular Proteins as Substrate Reacted with Diferent Proteinase FOOD SCIENCE 2004,25 (3) 36-43

不同蛋白酶水解酪蛋白类大分子底物的规律研究

作  者：
庞广昌;潘葳;陈庆森
单  位：
天津商学院生物工程系
关键词：
酪蛋白;水解度;大分子蛋白类底物;生物活性肽;蛋白酶
摘  要：
近年来,已有大量具有重要生物活性的短肽通过适当的蛋白酶水解营养或贮藏蛋白释放和辨认出来。这些蛋白资源十分丰富和廉价,通过水解这些蛋白质所获得的生物活性肽不仅价格便宜、安全性好、工艺简单,而且容易进行工业化生产。为了能够获得更高的生物活性肽得率,为生产和研究提供理论依据,本文开展了酶促蛋白水解制备生物活性肽的水解条件、底物浓度和水解度之间的关系研究。结果表明:当底物达到一定的浓度时,不仅其酶促反应速度会迅速下降,酶切位点和酶解产物也有明显不同。这些结果不符合米氏方程,显然酶解蛋白类大分子底物时酶和底物之间的作用比其他底物要复杂得多。
译  名：
Study on Hydrolysis Conditions of Macromolecular Proteins as Substrate Reacted with Diferent Proteinase
作  者：
PANG Guang-cang, PAN Wei, CHEN Qin-seng(Department of Biological Engineering,Tianjin University of Commerce,Tianjin 300134,China)
关键词：
casein; degree of hydrolysis(DH); substrates of macromolecular proteins; bioactive peptides; proteinase
摘  要：
Recently, scientists have found that milk and some other proteins were possible precursors of many different biologicalactive peptides. These peptides are inactive within the sequence of the precursor proteins and can be released from theprecursor when treated with proteinase under proper conditions such as pH, temperature and ionic concentration. Up to now,several kinds of biological peptides have been found from the proteolysis solution of nutritious or seed proteins. Because ofthese proteins were very cheap, rich in resources and safe for health, the bioactive peptides thereby have had commercialpotential, also been suitable to scale up. Therefore the degree of hydrolysis, digest conditions and the relationship between themacromolecule proteins substrates and the proteinases were investigated in several experiments in this paper. The resultsshowed that when the concentration of the substrate increased over some point, the rates of reactions will decrease on thecontrary. It was obviously deferent to the Michaelis-Menton Equation. It showed that the interactions between enzymes andsubstrates of macromolecular proteins might be more complex.

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