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从哈尔滨干肠中分离的肉葡萄球菌 RT6 的胞外蛋白酶的生化特性及其对肉蛋白的水解作用。

Biochemical properties of extracellular protease from Staphylococcus carnosus RT6 isolated from Harbin dry sausages, and its hydrolysis of meat proteins.

机构信息

College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang, China.

出版信息

J Food Sci. 2021 May;86(5):1642-1655. doi: 10.1111/1750-3841.15726. Epub 2021 Apr 29.

DOI:10.1111/1750-3841.15726
PMID:33928645
Abstract

The characteristics of the extracellular protease, produced by Staphylococcus carnosus RT6 isolated from Harbin dry sausages, and its hydrolysis of meat proteins were investigated. The protease was purified by ammonium sulfate, ion exchange, and gel filtration chromatography to obtain a 20.0 kDa extracellular protease. The protease reached maximal activity at pH 9.0 and 50 °C and was stable at pH 7.0 to 11.0 and 20 to 40 °C. Its protease activity was easily inhibited in the presence of Zn , Fe , and Fe . The enzymatic characterization of the protease revealed a V 49.50 U/ml·min, K 8.19 mg/ml, and the half-life = 28.06 min, ΔH  = 114.11 kJ/mol, ΔG  = 89.24 kJ/mol, and ΔS  = 77.00 J/mol·K at 50 °C. In addition, the protease hydrolyzed meat protein into small particles and produced soluble peptides. This study provides a basis for understanding the biochemical characteristics of the S. carnosus RT6 protease and its future application for fermented meat products.

摘要

从哈尔滨干肠中分离出的肉葡萄球菌 RT6 产生的细胞外蛋白酶的特性及其对肉蛋白的水解作用进行了研究。该蛋白酶通过硫酸铵沉淀、离子交换和凝胶过滤层析进行纯化,得到一种 20.0 kDa 的细胞外蛋白酶。该蛋白酶在 pH 9.0 和 50°C 时达到最大活性,在 pH 7.0 至 11.0 和 20 至 40°C 时稳定。其蛋白酶活性在存在 Zn 、Fe 和 Fe 时很容易被抑制。蛋白酶的酶学特性表明,V 49.50 U/ml·min、K 8.19 mg/ml,半衰期为 28.06 min,ΔH = 114.11 kJ/mol,ΔG = 89.24 kJ/mol,ΔS = 77.00 J/mol·K,在 50°C 时。此外,该蛋白酶将肉蛋白水解成小颗粒并产生可溶性肽。本研究为了解 S. carnosus RT6 蛋白酶的生化特性及其在发酵肉制品中的未来应用提供了依据。

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