高静水压对胰蛋白酶、嗜热菌蛋白酶和胃蛋白酶酶解β-乳球蛋白B的影响。

Effect of high hydrostatic pressure on the enzymic hydrolysis of beta-lactoglobulin B by trypsin, thermolysin and pepsin.

作者信息

Stapelfeldt H, Petersen P H, Kristiansen K R, Qvist K B, Skibsted L H

机构信息

Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Frederiksberg, Denmark.

出版信息

J Dairy Res. 1996 Feb;63(1):111-8. doi: 10.1017/s0022029900031587.

DOI:10.1017/s0022029900031587

PMID:8655736

Abstract

Hydrolysis of beta-lactoglobulin B (beta-lg B) by pepsin, a process slow at ambient conditions, is facilitated at a moderately high hydrostatic pressure such as 300 MPa, corresponding to an apparent volume of activation delta V# = -63 ml mol-1 at pH 2.5, 30 degrees C and gamma/2 = 0.16. Digestion of beta-lg by trypsin and thermolysin is likewise enhanced by pressure, and the pressure effect has been traced to pressure denaturation of beta-lg B, which by high-pressure fluorescence spectroscopy has been shown to have a large negative volume of reaction, delta V(o) = -98 ml mol-1, at pH 6.7, 30 degrees C and gamma/2 = 0.16. Pressure denaturation is only slowly reversed following release of pressure and the enhanced digestibility is maintained at ambient pressure for several hours.

摘要

在环境条件下，胃蛋白酶对β-乳球蛋白B（β-lg B）的水解过程较为缓慢，但在中等较高的静水压力（如300 MPa）下会得到促进，这相当于在pH 2.5、30℃和γ/2 = 0.16时，表观活化体积ΔV# = -63 ml mol-1。胰蛋白酶和嗜热菌蛋白酶对β-lg的消化同样会因压力而增强，并且压力效应已追溯到β-lg B的压力变性，通过高压荧光光谱法已表明，在pH 6.7、30℃和γ/2 = 0.16时，其具有很大的负反应体积，ΔV(o) = -98 ml mol-1。压力解除后，压力变性只能缓慢逆转，并且在环境压力下增强的消化性会维持数小时。