Abstract

A producer strain of Komagataella phaffii of recombinant beluga whale (Delphinapterus leucas) chymosin with a productivity of 80 mg/L was obtained, and the physico-chemical properties of the enzyme were studied for possible use in the food industry. The specific activity of the recombinant beluga chymosin was 55 IMCU/mg, which is significantly lower than that of recombinant bovine chymosin. The beluga whale chymosin has a high nonspecific proteolytic activity, which impaired its properties and ruled out its used in the food industry. Apparently, the amino acid substitutions K221M and K294Q are critically important and lead to a lower binding of casein micelles to the recombinant chymosin of the beluga whale.

中文翻译：

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Beluga Whale (Delphinapterus leucas) 凝乳酶在甲基营养酵母 Komagataella phaffii 中的产生及重组酶的特性

摘要

获得了产率为80mg/L的重组白鲸( Delphinapterus leucas )凝乳酶Komagataella phaffii生产菌株，并对该酶的理化性质进行了研究，以期在食品工业中的应用。重组白鲸凝乳酶的比活为55 IMCU/mg，明显低于重组牛凝乳酶。白鲸凝乳酶具有很高的非特异性蛋白水解活性，这削弱了其特性并排除了其在食品工业中的使用。显然，氨基酸取代 K221M 和 K294Q 至关重要，导致酪蛋白胶束与白鲸重组凝乳酶的结合较低。