2024-03-29T00:31:41Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/644792022-11-17T02:08:08Zhdl_2115_20046hdl_2115_138Kinetic properties and substrate inhibition of α-galactosidase from Aspergillus nigerLiao, JulanOkuyama, MasayukiIshihara, KeigoYamori, YoshinoriIki, ShigeoTagami, TakayoshiMori, HaruhideChiba, SeiyaKimura, Atsuoglycoside hydrolase family 27α-galactosidasesubstrate inhibitionsubstrate specificity400The recombinant AglB produced by Pichia pastoris exhibited substrate inhibition behavior for the hydrolysis of p-nitrophenyl -galactoside, whereas it hydrolyzed the natural substrates, including galactomanno-oligosaccharides and raffinose family oligosaccharides, according to the Michaelian kinetics. These contrasting kinetic behaviors can be attributed to the difference in the dissociation constant of second substrate from the enzyme and/or to the ability of the leaving group of the substrates. The enzyme displays the grater k(cat)/K-m values for hydrolysis of the branched -galactoside in galactomanno-oligosaccharides than that of raffinose and stachyose. A sequence comparison suggested that AglB had a shallow active-site pocket, and it can allow to hydrolyze the branched -galactosides, but not linear raffinose family oligosaccharides.Taylor & FrancisJournal Articleapplication/pdfhttp://hdl.handle.net/2115/64479https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/64479/1/Biosci.%20Biotechnol.%20Biochem.80-9_1747-1752.pdf0916-8451Bioscience biotechnology and biochemistry809174717522016-09enginfo:pmid/26856407info:doi/10.1080/09168451.2015.1136884This is an Accepted Manuscript of an article published by Taylor & Francis in Bioscience biotechnology and biochemistry on 09 Feb 2016, available online: http://wwww.tandfonline.com/10.1080/09168451.2015.1136884.author