Purification and properties of an exo-.ALPHA.-1,3-glucanase from Trichoderma viride.
Akira Tsunoda, Tameichiro Nagaki, Yoshiyuki Sakano, Tsuneo Kobayashi
Abstract
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Akira Tsunoda, Tameichiro Nagaki, Yoshiyuki Sakano, Tsuneo Kobayashi
Abstract
Open-access reader
An ƒ¿-1,3-glucanase was partially purified from Meicelase, a commercial cellulase prepa ration from T. viride, and its properties were studied.Cellulase in the crude enzyme was removed by adsorption on cellulose powder, and ƒ¿-1,3-glucanase was purified through salting out with ammonium sulfate, chromatographies on DEAE-Sephadex, hydroxylapatite and
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An ƒ¿-1,3-glucanase was partially purified from Meicelase, a commercial cellulase prepa ration from T. viride, and its properties were studied.Cellulase in the crude enzyme was removed by adsorption on cellulose powder, and ƒ¿-1,3-glucanase was purified through salting out with ammonium sulfate, chromatographies on DEAE-Sephadex, hydroxylapatite and
Key concepts: Sephadex, Chemistry, Trichoderma viride, Glucanase, Cellulase, Chromatography, Size-exclusion chromatography, Enzyme