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[Production and some properties of a beta-glucanase from Trichoderma sp. GXC].

Junyong Sun, W Li, Shaohua Gu

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Abstract

The factors affecting Trichoderma sp. GXC for beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.73) production have been investigated, the optimal conditions were that carbon and nitrogen sources were bran and ammonium sulfate, respectively, initial pH 4.0-5.0, shaken at 30 degrees C for 44 h. beta-glucanase was purified to electrophoretic homogeneity by using ammonium sulfate precipitation, Sephadex G-100 and DEAE-Sephadex A-50 chromatography. It's molecular weight was 35 kD by SDS-PAGE, and the enzyme functioned optimally at pH6.0 and 50 degrees C, respectively. In addition, the enzyme was stable at pH 4.0-5.0 and below 40 degrees C. The beta-glucanase activity was significantly inhibited by Fe3+ and stimulated by Co2+, respectively.

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What this paper is about

The factors affecting Trichoderma sp. GXC for beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.73) production have been investigated, the optimal conditions were that carbon and nitrogen sources were bran and ammonium sulfate, respectively, initial pH 4.0-5.0, shaken at 30 degrees C for 44 h. beta-glucanase was purified to electrophoretic homogeneity by using ammonium sulfate precipitation, Sephadex G-100 and DEAE-Sephadex A-50 chromatography. It's molecular weight was 35 kD by SDS-PAGE, and the enzyme functioned optimally at pH6.0 and 50 degrees C, respectively. In addition, the enzyme was stable at pH 4.0-5.0 and below 40 degrees C. The beta-glucanase activity was significantly inhibited by Fe3+ and stimulated by Co2+, respectively.

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Available abstract

The factors affecting Trichoderma sp. GXC for beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.73) production have been investigated, the optimal conditions were that carbon and nitrogen sources were bran and ammonium sulfate, respectively, initial pH 4.0-5.0, shaken at 30 degrees C for 44 h. beta-glucanase was purified to electrophoretic homogeneity by using ammonium sulfate precipitation, Sephadex G-100 and DEAE-Sephadex A-50 chromatography. It's molecular weight was 35 kD by SDS-PAGE, and the enzyme functioned optimally at pH6.0 and 50 degrees C, respectively. In addition, the enzyme was stable at pH 4.0-5.0 and below 40 degrees C. The beta-glucanase activity was significantly inhibited by Fe3+ and stimulated by Co2+, respectively.

Key concepts: Ammonium sulfate precipitation, Glucanase, Ammonium sulfate, Sephadex, Chemistry, Bran, Chromatography, Trichoderma reesei

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