An effective immobilization of β-glucosidases by partly cross-linking enzyme aggregates. Issue 9 (3rd October 2022)

• Record Type: Journal Article
• Authors: Deng, Yuefeng; Ouyang, Jie; Liu, Hu; Wang, Jianjun; Zhu, Yihui; Chen, Ziqian; Yang, Chengli; Li, Dali; Ma, Kefeng
• Is Part Of: Preparative biochemistry & biotechnology. Volume 52:Issue 9(2022)
• Page Start: 1035
• Page End: 1043
• Publication Date: 2022-10-03
• Subjects: β-Glucosidase -- pCLEAs -- immobilization -- montmorillonite; Biochemistry -- Technique -- Periodicals; Biotechnology -- Technique -- Periodicals; Biochemistry -- methods -- Periodicals; Biotechnology -- methods -- Periodicals; 660.6
• DOI: 10.1080/10826068.2021.2024848
• Languages: English
• ISSNs: 1082-6068

Abstract

Abstract: Enzyme immobilization provides ideal operating conditions for enzymes stabilization and sustainable recycling. In this work, as a kind of clay material, montmorillonite (MTL) was chosen for immobilizing the β-glucosidase extracted from Agrocybe aegirit . The immobilized β-glucosidase via partly cross-linking enzyme aggregates (pCLEAs) formed by self-catalysis provided biocatalysts with satisfactory thermal and pH stability. Compared to the glutaraldehyde cross-linked, the immobilized β-glucosidase (β-G-pCLEAs@MTL) exhibited significantly higher immobilization efficiency ( IE ) and immobilization yield ( IY ), which were 80.6% and 76.9%, respectively. The β-G-pCLEAs@MTL also showed better stability and preferable reusability. And the activity of the β-G-pCLEAs@MTL remained 85.0% after 5 cycles and 74.7% after 10 cycles. Therefore, the method based on the pre- crosslinking to form pCLEAs and after-immobilization can effectively improve IY and IE . In addition, MTL seems to be a good alternative carrier to immobilize other enzymes for industrial application.