title: Purification and characterization of α-galactosidase from white chickpea (Cicer arietinum).
abstract: Glycosylated α-galactosidase (melibiase) has been purified from white chickpea ( Cicer arietinum ) to 340-fold with a specific activity of 61 units/mg. Cicer α-galactosidase showed a M(r) of 45 kDa on SDS-PAGE and by MALDI-TOF. The optimum pH and temperature with pNPGal were 4.5 and 50 °C, respectively. The K(m) for hydrolysis of pNPGal was 0.70 mM. Besides hydrolyzing the pNPGal, Cicer α-galactosidase also hydrolyzed natural substrates such as melibiose, raffinose, and stachyose very effectively; hence, it can be exploited commercially for improving the nutritional value of soy milk. Galactose was found to be a competitive inhibitor. The property of this enzyme to cleave the terminal galactose residues can be utilized for converting the group B erythrocytes to group O erythrocytes.
authors.affiliation: School of Biotechnology, Faculty of Science, Banaras Hindu University, Varanasi 221005, India.
authors.forename: Neelesh
authors.initials: N
authors.lastname: Singh
authors.forename: Arvind M
authors.initials: AM
authors.lastname: Kayastha
mesh_terms: D001789:Blood Group Antigens / Q000378:metabolism; D029863:Cicer / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D009844:Oligosaccharides / Q000378:metabolism; D011887:Raffinose / Q000737:chemistry; D012639:Seeds / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature; D000519:alpha-Galactosidase / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D001789:Blood Group Antigens; D008670:Metals; D009844:Oligosaccharides; D000519:alpha-Galactosidase; D011887:Raffinose