Literature DB >> 35184224

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

Tiantian Li1, Xiaowu Gong2, Gaoshan Yang1, Qin Li1, Jin Huang1,3, Na Zhou4, Xin Jia1.   

Abstract

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 (t1/2) and inactivation energy (Ed) 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.

Entities:  

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

Mesh:

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Year:  2022        PMID: 35184224     DOI: 10.1007/s00449-022-02704-0

Source DB:  PubMed          Journal:  Bioprocess Biosyst Eng        ISSN: 1615-7591            Impact factor:   3.210


  28 in total

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