Rutinosidase and other diglycosidases: Rising stars in biotechnology.
Aspergillus
Diglycosidase
Glycobiology
Primeverosidase
Rutinosidase
Transglycosylation
Journal
Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708
Informations de publication
Date de publication:
11 2023
11 2023
Historique:
received:
10
01
2023
revised:
09
07
2023
accepted:
16
07
2023
medline:
13
9
2023
pubmed:
23
7
2023
entrez:
22
7
2023
Statut:
ppublish
Résumé
Diglycosidases are a special class of glycosidases (EC 3.2.1) that catalyze the separation of intact disaccharide moieties from the aglycone part. The main diglycosidase representatives comprise rutinosidases that cleave rutinose (α-l-Rha-(1-6)-β-d-Glc) from rutin or other rutinosides, and (iso)primeverosidases processing (iso)primeverosides (d-Xyl-(1-6)-β-d-Glc), but other activities are known. Notably, some diglycosidases may be ranked as monoglucosidases with enlarged substrate specificity. Diglycosidases are found in various microorganisms and plants. Diglycosidases are used in the food industry for aroma enhancement and flavor modification. Besides their hydrolytic activity, they also possess pronounced synthetic (transglycosylating) capabilities. Recently, they have been demonstrated to glycosylate various substrates in a high yield, including peculiar species like inorganic azide or carboxylic acids, which is a unique feature in biocatalysis. Rhamnose-containing compounds such as rutinose are currently receiving increased attention due to their proven activity in anti-cancer and dermatological experimental studies. This review demonstrates the vast and yet underrated biotechnological potential of diglycosidases from various sources (plant, microbial), and reveals perspectives on the use of these catalysts as well as of their products in biotechnology.
Identifiants
pubmed: 37481095
pii: S0734-9750(23)00124-6
doi: 10.1016/j.biotechadv.2023.108217
pii:
doi:
Substances chimiques
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
108217Informations de copyright
Copyright © 2023 Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare no conflicts of interest.