School of Chemical Sciences and Food Technology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor Malaysia.
School of biosciences and biotechnology, Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor Malaysia.
J Food Sci Technol. 2014 Mar;51(3):467-75. doi: 10.1007/s13197-011-0526-6. Epub 2011 Sep 13.
This study was conducted to evaluate the kinetic characteristics of proteolytic activity of proteases on Channa striatus protein fractions. Degree of hydrolysis (DH), amino acid composition and kinetic parameters of sarcoplasmic and myofibrillar proteins were investigated when incubated with proteinase K and thermolysin, separately. After 30 min incubation with proteases, a decrease in DH of sarcoplasmic protein was observed whereas, hydrolysis of myofibrillar protein with proteases took 2 h with an increase in DH. The major amino acids were glutamic acid (16.6%) in thermolysin- myofibrillar hydrolysate followed by aspartic acid (11.1%) in sarcoplasmic protein fraction with no enzyme treatment and lysine (10%) in thermolysin-myofibrillar hydrolysate. The apparent Michaelis constant of proteinase K was lower than thermolysin for both sarcoplasmic and myofibrillar proteins. However, rate of turnover and enzyme efficiency suggested that sarcoplasmic and myofibrillar proteins are suitable substrates for proteinase K and thermolysin hydrolytic reaction, respectively.
本研究旨在评估蛋白酶对纹缟鯙蛋白组分的蛋白水解活性的动力学特性。当分别用蛋白酶 K 和胰凝乳蛋白酶孵育时,研究了肌浆蛋白和肌原纤维蛋白的水解度(DH)、氨基酸组成和动力学参数。用蛋白酶孵育 30 分钟后,观察到肌浆蛋白的 DH 降低,而用蛋白酶水解肌原纤维蛋白则需要 2 小时,DH 增加。主要氨基酸为天冬氨酸(11.1%),无酶处理的肌浆蛋白部分,随后是谷氨酸(16.6%)和赖氨酸(10%),胰凝乳蛋白酶-肌原纤维水解物。对于肌浆蛋白和肌原纤维蛋白,蛋白酶 K 的表观米氏常数均低于胰凝乳蛋白酶。然而,周转率和酶效率表明,肌浆蛋白和肌原纤维蛋白分别适合蛋白酶 K 和胰凝乳蛋白酶水解反应的底物。