ABSTRACT Molecular weights of trypsin, chymotrypsin, and lipase from anterior intestine and pyloric caeca of Totoaba macdonaldi were evaluated, as well as optimum temperature and pH for activity of the proteases. Trypsin was 24.1 kDa and effectively hydrolyzed Nα-benzoyl-DL-arginine 4-nitroanilide hydrochloride at optimum pH and temperature of 8 and 65°C, respectively. Chymotrypsin was 25.9 kDa and showed higher hydrolytic activity for N-benzoyl-L-tyrosine ethyl ester at pH 8 and 45°C, with a wider range of statistically similar activity values. Two pancreatic lipases of 70.2 and 47.5 kDa were detected, which could be the uncleaved and the final form of a colipase-dependent pancreatic lipase, since enzyme activity was detected without supplementation of bile salts and supplementing them inhibited activity.

中文翻译：

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麦克唐纳石首鱼消化道中胰蛋白酶、糜蛋白酶和脂肪酶的活性和部分表征

摘要 评估了来自 Totoaba macdonaldi 的前肠和幽门盲囊的胰蛋白酶、糜蛋白酶和脂肪酶的分子量，以及蛋白酶活性的最适温度和 pH 值。胰蛋白酶为 24.1 kDa，可在最佳 pH 值和温度分别为 8 和 65°C 时有效水解 Nα-苯甲酰基-DL-精氨酸 4-硝基苯胺盐酸盐。胰凝乳蛋白酶为 25.9 kDa，在 pH 8 和 45°C 下对 N-苯甲酰基-L-酪氨酸乙酯显示出更高的水解活性，具有更广泛的统计相似活性值。检测到两种 70.2 kDa 和 47.5 kDa 的胰脂肪酶，它们可能是未裂解的和最终形式的辅脂肪酶依赖性胰脂肪酶，因为在没有补充胆汁盐的情况下检测到酶活性，并且补充它们抑制了活性。