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International Journal of Biological Macromolecules

International Journal of Biological Macromolecules

IF: 7.7
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Compartmentalized co-immobilization of cellulase and a cellobiose phosphorylase within a zeolitic imidazolate framework efficiently synthesizes 1-p-Glc?…

Published:10 December 2024 DOI: 10.1016/j.ijbiomac.2024.138653 PMID: 39667458
Jingjie Gao,?Shaowei Bai,?Fan Wang,?Liangzhen Yang,?Yufeng Hu,?Yuhuan Yang,?Bing Bai,?Zuoming Zhang

Abstract

Enzymatic glycosylation is an efficient and biocompatible approach to enhance natural product bioavailability. Cellobiose phosphorylase, a novel glycosyltransferase, utilizes 1-phospho-glucose (1-p-Glc) as a glycosyl donor for regioselective glycosylation of various natural substrates. However, the high cost of 1-p-Glc limits the economic feasibility of the process. Thus, a dual-enzyme cascade system involving cellulase AcCel9A and cellobiose phosphorylase CbCBP using a co-immobilization strategy was developed to overcome this challenge. The system utilizes low-cost carboxymethyl cellulose (CMC) for continuous 1-p-Glc production, which was then used in the fluorodeoxy glucose (FDG) glycosylation to generate fluorodeoxy cellobiose (FDC), which potentially traces fungal infections. The compartmentalized co-immobilization of the two enzymes within the internal and external regions of a porous zeolitic imidazolate framework-8 (ZIF-8) carrier enhanced the overall stability of the dual-enzyme system. The protein concentration in the co-immobilized enzyme carrier is approximately 65?mg/g. The immobilized enzymes retained approximately 63.3?% activity after seven reuse cycles and 74?% catalytic efficiency after 12?days of storage at room temperature. Therefore, the developed co-immobilized multi-enzyme system holds significant potential for industrial biocatalysis applications.

Substances (1)

Materials
Procduct Name CAS Molecular Formula Supplier Price
Fluorescein isothiocyanate 27072-45-3 C21H11NO5S 213 suppliers $42.90-$1250.00

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