Paper Title:
Substrate Specificities of α-Galactosidase from Rice
  Abstract

The α-galactosidase from rice cleaved not only α-D-galactosyl residues from the non-reducing end of substrates such as melibiose, raffinose and stachyose, but also liberated the terminal galactosyl residues attached O-6 position of the reducing-end mannosyl residue in mannobiose and mannotriose. In addition, the enzyme tore off the stubbed galactosyl residues attached inner-mannosyl residues in mannopentaose. It also could catalyze efficient degalactosylation of galactomannans, such as guar gum and locust bean gum.

  Info
Periodical
Advanced Materials Research (Volumes 183-185)
Chapter
Environmental Biotechnology
Edited by
Yanguo Shi and Jinlong Zuo
Pages
447-451
DOI
10.4028/www.scientific.net/AMR.183-185.447
Citation
S. H. Li, M. P. Zhu, T. P. Li, "Substrate Specificities of α-Galactosidase from Rice", Advanced Materials Research, Vols. 183-185, pp. 447-451, 2011
Online since
January 2011
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