The Loop Regions and Substrate Specificity
of GH 27 Familiy α-Galactosidases
Volume 1 - Issue 1
Canfang Niu and Peilong Yang’s*
-
Author Information
Open or Close
- National Engineering Research Center of Biological Feed, Key Laboratory for Feed, Biotechnology of the Ministry of Agriculture, Feed
Research Institute, Chinese Academy of Agricultural Sciences, Beijing, P.R China
*Corresponding author:
Peilong Yang’s, National Engineering Research Center of Biological Feed, Key Laboratory for Feed, Biotechnology
of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, P R China
Received: April 09, 2018; Published: April 17, 2018
DOI: 10.32474/SJFN.2018.01.000102
Full Text
PDF
To view the Full Article Peer-reviewed Article PDF
Abstract
α-Galactosidases as natural biocatalysts have important application value in various industries. In this paper, we reviewed their
physiological functions, biological sources, classification, and protein structure and substrate specificity relationships of Glycoside
hydrolase (GH) family 27, aiming at providing references for related experiments and studies.
Keywords: GH27α-Galactosidase; Loop region; Substrate specificity; Thermo stability; Stability at low pH 29
Abbrevations: GH: Glycoside Hydrolase
Abstract|
Introduction|
Acknowledgement|
References|