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- W613672182 abstract "Differentiating activity assays of cellulase-components (all specific for β-1,4 glucosidic linkages) are described using chromogenic derivatives of lactose and the cellodextrins. They proved to be valuable not only in specificity studies of these enzymes, but also as active site probes. An affinity chromatographic method for rapid isolation of some of these enzymes was also developed. New information on the domain structure of two cellobiohydrolases from Trichoderma reesei (CBH I and CBH II) resulted from structure-function investigations based on partial proteolysis and physical measurements. A cellulose-binding domain (C- or N-terminal) was separated from the core-enzymes, containing the active (hydrolytic) sites. In the tadpole structure of the intact enzymes—as deduced from small-angle X-ray scattering—the binding peptides protrudes from their cores as flexible tails. Study of adsorption onto and hydrolysis of microcrystalline cellulose (Avicel) led to new insights into the functional role of these domains and the synergism observed between CBH I and CBH II." @default.
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- W613672182 date "1989-07-31" @default.
- W613672182 modified "2023-09-25" @default.
- W613672182 title "Specific Assays, Purification, and Study of Structure—Activity Relationships of Cellulolytic Enzymes" @default.
- W613672182 doi "https://doi.org/10.1021/bk-1989-0399.ch041" @default.
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