摘要
研究了里氏木霉GXCβ -葡聚糖酶的稳定性。结果发现 :β-葡聚糖酶粗酶液的稳定性高于纯酶液 ,两者的耐热温度分别为 70℃和 6 0℃ ,其pH稳定范围都为 3.0～ 5 .0。Cu2 +,Mn2 +和Fe3+对酶有抑制作用 ,Zn2 +和Co2 +有激活作用 ,其他离子Ca2 +,Mg2 +,Fe2 +和K+在不同浓度条件下对β -葡聚糖酶有不同的作用。胰蛋白酶和胃蛋白酶对 β
In a study of the stability of β-glucanase derived from Trichoderma reesei (strain GXC),the crude enzyme of β-glucanase appeared more stable than its purified enzyme,being tolerant to a high temperature of 70℃ and 60℃,respectively.The pH range for the stability of both was 3.0～5.0 Cu 2+ ,Mn 2+ and Fe 3+ showed an inhibitory effect on its activity while Zn 2+ and Co 2+ a stimulating effect.Ca 2+ ,Mg 2+ ,Fe 2+ and K +varied in their effects on the stability of the enzyme with different concentrations.The activity of β-glucanase seemed insensitive to pepsin and trypsin.
出处
《西南农业大学学报（自然科学版）》
CSCD
北大核心
2001年第2期97-99,共3页
Journal of Southwest Agricultural University
基金
高等学校骨干教师资助计划资助
国家自然科学基金 !(30 0 0 0 1 1 8)
浙江省自然科学基金! (39940 9)
浙江省教委项目
