Unknown

Dataset Information

0

Cold-Active ?-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.


ABSTRACT: ?-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of ?-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active ?-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic ?-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active ?-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries.

SUBMITTER: Mangiagalli M 

PROVIDER: S-EPMC7832830 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.

Mangiagalli Marco M   Lotti Marina M  

Marine drugs 20210119 1


β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in bio  ...[more]

Similar Datasets

| S-EPMC3973953 | biostudies-literature
| S-EPMC8445988 | biostudies-literature
| S-EPMC5016527 | biostudies-literature
| S-EPMC7022595 | biostudies-literature
| S-EPMC4064286 | biostudies-literature
| S-EPMC3741176 | biostudies-literature
| S-EPMC7960840 | biostudies-literature
| S-EPMC8540142 | biostudies-literature
| S-EPMC10441238 | biostudies-literature
| S-EPMC5342196 | biostudies-literature