Abstract
Abstract The first three-dimensional structures of β-1,4-glycanases and β-glycosidases are beginning to be reported, but because of the difficulties associated with crystallization relatively few have been solved to date. Most of the engineering of these enzymes is based on sequence determination and alignment, and on inhibitor studies. The modular structures of many β-1,4-glycanases and β-glycosidases have facilitated the analysis of domain function. Recent work has demonstrated that the cellulose-binding domains of some of these enzymes can be used as affinity tags for protein purification and enzyme immobilization.
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