Raw Starch-digestive Chitin-immobilized Amylase from a Protease-Glycosidase-less Mutant of Aspergillus awamori var. kawachi
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概要
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The α-amylase and glucoamylase produced by a protease-, glycosidase-less mutant HF-15 of Aspergillus awamori var. kawachi were found to be adsorbable onto chitin. This adsorption was pH-independent, different from the adsorption onto raw corn starch. The binding between amylases and chitin was so tight that a chitin-immobilized amylase was obtained without the aid of a cross linking agent, glutaraldehyde, and it retained more than 90% of the original activity of the free enzyme. The immobilized amylase digested gelatinized potato starch, glycogen and even raw corn starch to the same high extent as glucose similar to the free enzyme, but it was different from the unbound crude enzyme in the lack of transglucosidase activity, and slightly different in pH- and thermo-stabilities. An experiment using the immobilized amylase for alcohol fermentation demonstrated the possibility of recycling the enzyme for raw starch saccharification.
- 社団法人 日本農芸化学会の論文
著者
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Hayashida Shinsaku
Department of Agricultural Chemistry, Faculty of Agriculture, Kyushu University
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Hayashida Shinsaku
Department Of Agricultural Chemistry
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FLOR Perfecto
Department of Agricultural Chemistry, Kyushu University
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