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金枪鱼废弃物中的凝乳酶作为一种凝乳酶替代品

Milk-coagulating enzymes of tuna fish waste as a rennet substitute.

作者信息

Tavares J F, Baptista J A, Marcone M F

机构信息

University of Azores, Portugal.

出版信息

Int J Food Sci Nutr. 1997 May;48(3):169-76. doi: 10.3109/09637489709012590.

Abstract

Extraction and activation of the tuna zymogen is influenced by temperature, pH, salt concentration and freshness of the stomach tissue. The presence of 25% NaCl in the extraction process markedly enhanced the yield of tuna gastric enzyme. The milk-coagulating time for both tuna protease and rennet, at an incubation temperature of 32 degrees C, was dependent, at similar level, on the pH (5.5-6.4) of the milk as a substrate. Tuna protease was less sensitive to losses of activity than rennet at pH values above 6.4. Both enzymes became unstable beyond pH 7.0 and completely lost their activities at pH 8.0. The purpose of this study was to determine the best conditions for recovery of the fish enzyme and to compare its behavior to that of rennet.

摘要

金枪鱼酶原的提取和激活受温度、pH值、盐浓度和胃组织新鲜度的影响。提取过程中25%氯化钠的存在显著提高了金枪鱼胃酶的产量。在32℃的孵育温度下,金枪鱼蛋白酶和凝乳酶的凝乳时间在相似水平上取决于作为底物的牛奶的pH值(5.5-6.4)。在pH值高于6.4时,金枪鱼蛋白酶比凝乳酶对活性损失更不敏感。两种酶在pH值高于7.0时变得不稳定,在pH值8.0时完全失去活性。本研究的目的是确定回收鱼酶的最佳条件,并将其行为与凝乳酶进行比较。

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