伪-Amylase from wheat (Triticum aestivum) seeds: Its purification, biochemical attributes and active site studies
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文摘

Wheat 伪-amylase was purified to homogeneity and its identity confirmed by MALDI-TOF.

Biochemical characterisation revealed resistance to SDS denaturation at low concentrations.

High kcat objectifies wheat 伪-amylase for starch based and related industries.

Chemical modification studies showed histidine presence at the enzyme’s active site.

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