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One-step immobilization-purification of enzymes by carbohydrate-binding module family 56 tag fusion

Author:
Qin, Zhen, Lin, Si, Qiu, Yongjun, Chen, Qiming, Zhang, Yin, Zhou, Jiachun, Zhao, Liming
Source:
Food chemistry 2019 v.299 pp. 125037
ISSN:
0308-8146
Subject:
adsorption, beta-glucans, biocatalysis, carbohydrate binding, chitosanase, curdlan, environmental impact, food industry, hydrogen, immobilized enzymes
Abstract:
Immobilization of enzymes is an essential strategy with outstanding prospects in biocatalytic processes. Nontoxic, inexpensive immobilized enzyme approach is especially important for food enzymes. We here demonstrate that a carbohydrate-binding module family 56 domain (CBM56-Tag) mediates the immobilization of fusion enzymes with the curdlan (β-1,3-glucan) particle support, thereby enabling the one-step immobilization-purification of target enzymes. CBM56-Tag exhibits an immunoglobulin-like β-sandwich fold, which can be adsorbed by curdlan via hydrogen bond-mediated binding. The maximum adsorption capacity of a fusion chitosanase (CBM56-GsCsn46A) on curdlan is 50.72 mg/g. The immobilized enzyme could be directly used in the packed-bed reactor. This immobilization strategy utilizes a natural polysaccharide without any treatment, avoiding the negative environmental effects. Moreover, the one step immobilization-purification simplifies the purification step, which reduces the use of chemicals. Our study provides a nontoxic and inexpensive immobilization strategy for the biocatalytic reaction in food industry.
Agid:
6474998