Version 1
: Received: 22 April 2024 / Approved: 23 April 2024 / Online: 23 April 2024 (11:58:13 CEST)
How to cite:
Jaiswal, N.; Jaiswal, P. Thermostable α-Amylases and Laccases: Paving the Way for Sustainable Industrial Applications.. Preprints2024, 2024041488. https://doi.org/10.20944/preprints202404.1488.v1
Jaiswal, N.; Jaiswal, P. Thermostable α-Amylases and Laccases: Paving the Way for Sustainable Industrial Applications.. Preprints 2024, 2024041488. https://doi.org/10.20944/preprints202404.1488.v1
Jaiswal, N.; Jaiswal, P. Thermostable α-Amylases and Laccases: Paving the Way for Sustainable Industrial Applications.. Preprints2024, 2024041488. https://doi.org/10.20944/preprints202404.1488.v1
APA Style
Jaiswal, N., & Jaiswal, P. (2024). Thermostable α-Amylases and Laccases: Paving the Way for Sustainable Industrial Applications.. Preprints. https://doi.org/10.20944/preprints202404.1488.v1
Chicago/Turabian Style
Jaiswal, N. and Pundrik Jaiswal. 2024 "Thermostable α-Amylases and Laccases: Paving the Way for Sustainable Industrial Applications." Preprints. https://doi.org/10.20944/preprints202404.1488.v1
Abstract
The growing demand in industrial and biotechnological settings for more efficient enzymes with enhanced biochemical features, particularly thermostability and thermotolerance, necessitates a timely response. Renowned for their versatility, thermostable enzymes, offer significant promise across a range of applications, including agricultural, medicinal, and biotechnological domains. This comprehensive review summarizes the structural attributes, catalytic mechanisms, and the relationships between structure and function of two major classes of thermostable enzymes: α-amylases and laccases. These enzymes serve as valuable models for understanding the structural basis of protein thermostability. Commercial significance of these enzymes and researchers' interest in further optimization and innovation, this article can greatly contribute to ongoing research on thermostable enzymes and aiding industries in optimizing production processes. It also give insights to the exploration of suitable strategies and factors for enhancing thermostability, resulting in heightened multipronged stability and notable enhancements in the enzymes’ industrial applicability.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
