Cross-linked enzyme aggregates (CLEAs) of cellulase with improved catalytic activity, adaptability and reusability.

Publisher: Springer-Verlag Country of Publication: Germany NLM ID: 101088505 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1615-7605 (Electronic) Linking ISSN: 16157591 NLM ISO Abbreviation: Bioprocess Biosyst Eng Subsets: MEDLINE

Original Publication: Berlin, Germany : Springer-Verlag, 2001-

Cellulase* ; Enzymes, Immobilized*/metabolism; Cross-Linking Reagents ; Enzyme Stability ; Glutaral ; Temperature

In this study, cross-linked cellulase aggregates (C-CLEAs) were synthesized by precipitation of cellulase with ammonium sulfate and then cross-linking with glutaraldehyde. The results revealed that the optimal pH of C-CLEAs shifted toward a more acidic environment by 2.0 pH units, and the optimal temperature shifted toward higher temperature by 20 °C after immobilization. The half-life (t 1/2 ) and inactivation energy (E d ) values of the C-CLEAs were 5.98 times and 1.93 times than that of free cellulase, respectively. Moreover, the C-CLEAs can also maintain about 65.22% of activity after 10 cycles and 63.03% of activity after storage for 56 days at 4 °C. Enzymatic hydrolysis of carboxymethylcellulose sodium and corncob in C-CLEAs system verified that the C-CLEAs performed better than free cellulase (P < 0.01).
(© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.)

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SHYL-DK201803 General Science and Technology Project of "Double First Class University Plan" Construction of Shihezi University; 21464011 National Natural Science Foundation of China

Keywords: Catalytic activity; Cross-linked cellulase aggregates; Enzymatic saccharification; Thermal stability

0 (Cross-Linking Reagents)
0 (Enzymes, Immobilized)
EC 3.2.1.4 (Cellulase)
T3C89M417N (Glutaral)

Date Created: 20220220 Date Completed: 20220426 Latest Revision: 20220426

20250114

10.1007/s00449-022-02704-0

35184224