Cold-adapted enzymes: mechanisms, engineering and biotechnological application

Abstract Most cold-adapted enzymes display high catalytic activity at low temperatures (20–25 °C) and can still maintain more than 40–50% of their maximum activity at lower temperatures (0–10 °C) but are inactivated after a moderate increase in temperature. The activity of some cold-adapted enzymes increases significantly in the presence of high salt concentrations and metal ions. Interestingly, we also observed that some cold-adapted enzymes have a wide range of optimum temperatures, exhibiting not only maximum activity under low-temperature conditions but also the ability to maintain high enzyme activity under high-temperature conditions, which is a novel feature of cold-adapted enzymes. This unique property of cold-adapted enzymes is generally attractive for biotechnological and industrial applications because these enzymes can reduce energy consumption and the chance of microbial contamination, thereby lowering the production costs and maintaining the flavor, taste and quality of foods. How high catalytic activity is maintained at low temperatures remains unknown. The relationship between the structure of cold-adapted enzymes and their activity, flexibility and stability is complex, and thus far, a unified explanation has not been provided. Herein, we systematically review the sources, catalytic characteristics and cold adaptation of enzymes from four enzymes categories systematically and discuss how these properties may be exploited in biotechnology. A thorough understanding of the properties, catalytic mechanisms, and engineering of cold-adapted enzymes is critical for future biotechnological applications in the detergent industry and food and beverage industries..

Medienart:

Artikel

Erscheinungsjahr:

2023

Erschienen:

2023

Enthalten in:

Zur Gesamtaufnahme - volume:46

Enthalten in:

Bioprocess and biosystems engineering - 46(2023), 10 vom: 24. Juli, Seite 1399-1410

Sprache:

Englisch

Beteiligte Personen:

Liu, Yan [VerfasserIn]
Jia, Kaizhi [VerfasserIn]
Chen, Hongyang [VerfasserIn]
Wang, Zhulin [VerfasserIn]
Zhao, Wei [VerfasserIn]
Zhu, Liwen [VerfasserIn]

Links:

Volltext [lizenzpflichtig]

Themen:

Cold-adapted
Protein flexibility
Protein structure
Stability

Anmerkungen:

© The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

doi:

10.1007/s00449-023-02904-2

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

OLC2145561668