Mischke S
Systematic Botany and Mycology Laboratory, U.S. Department of Agriculture, Beltsville, Maryland 20705-2350, USA.
Microbios. 1996;87(352):175-83.
Four chromogenic substrates were compared, and methods were developed for measuring protease activity from fungi. Digestion of azoalbumin, a water-soluble substrate, resulted in dye release most closely proportional to enzyme activity. Substrates insoluble in water were advantageous for time-course studies, and azocoll was more sensitive to digestion and easier to handle than hide powder azure. The optimal pH was 7 for measurement of extracellular protease activity from the Trichoderma strains. Addition of calcium or serine protease inhibitors did not affect crude protease activity. The optimized protocol was used to demonstrate that specific activity of proteases produced by the strains of Trichoderma tested did not correlate with their known biocontrol ability.
比较了四种显色底物，并开发了测量真菌蛋白酶活性的方法。水溶性底物偶氮白蛋白的消化导致染料释放与酶活性最密切相关。不溶于水的底物有利于进行时间进程研究，并且偶氮胶原比皮粉天蓝对消化更敏感且更易于处理。木霉菌株胞外蛋白酶活性测量的最佳pH值为7。添加钙或丝氨酸蛋白酶抑制剂不影响粗蛋白酶活性。使用优化的方案证明，所测试的木霉菌株产生的蛋白酶的比活性与其已知的生物防治能力无关。
