Naringinases: occurrence, characteristics, and applications

Mini-Review

DOI: 10.1007/s00253-011-3176-8

Cite this article as:
Ribeiro, M.H. Appl Microbiol Biotechnol (2011) 90: 1883. doi:10.1007/s00253-011-3176-8

Abstract

Naringinase, an enzyme complex, is commercially attractive due to its potential usefulness in pharmaceutical and food industries. It is of particular interest in the biotransformation of steroids, antibiotics, and mainly of glycosides hydrolysis. Moreover, it can be used in citrus juices debittering and wine industries. Naringinase expresses activity on α-l-rhamnosidase and β-d-glucosidase. Many natural glycosides, including naringin, rutin, quercitrin, hesperidin, diosgene, and ter-phenyl glycosides, containing terminal α-rhamnose and β-glucose can act as substrates of naringinase. The sources, production, activity, biochemical properties, and substrate specificity of naringinase are reviewed, along with a description of the enzymatic deglycosylation systems and applications, concluding with the identification of areas which need further extensive studies.

Keywords

Naringinase α-l-Rhamnosidase β-d-Glucosidase Glycosides Deglycosylation Immobilization 

Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  1. 1.Research Institute for Medicines and Pharmaceutical Sciences (i.Med-UL), Faculty of PharmacyUniversity of LisbonLisbonPortugal