Beta-glucosidase of a white-rot fungus Trametes gibbosa.

Biochemistry international Pub Date : 1992-12-01
B Bhattacharjee, A Roy, A L Majumder
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Abstract

Extracellular beta-glucosidase was purified from a white-rot fungus, Trametes gibbosa by 50% ammonium sulphate saturation and Sephadex G-100 column chromatography. It showed maximum activity towards p-nitrophenyl- beta-D- glucopyranoside (pNpG). The pH optimum was 3.5. Temperature optimum was 40 degrees C but shifted to 50 degrees C on preincubation with pNpG. Hg2+, Fe3+ and Cu2+ strongly inhibited the activity. The enzyme was competitively inhibited by glucose with a Ki of 5.2 mM. The apparent molecular mass as determined by gel filtration chromatography was 640 kDa.

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白腐真菌赤霉素的β -葡萄糖苷酶。
采用50%硫酸铵饱和和Sephadex G-100柱层析法从白腐菌Trametes gibbosa中纯化细胞外β -葡萄糖苷酶。对对硝基苯- β - d -葡萄糖吡喃苷(pNpG)的活性最大。最适pH为3.5。最适温度为40℃,但pNpG预孵育后温度为50℃。Hg2+、Fe3+和Cu2+对活性有较强的抑制作用。该酶被葡萄糖竞争性抑制,Ki为5.2 mM,凝胶过滤层析测定表观分子质量为640 kDa。
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