4.4 Article

Molecular Cloning and Characterization of a Novel Exo-β-1,3-Galactanase from Penicillium oxalicum sp. 68

Journal

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume 32, Issue 8, Pages 1064-1071

Publisher

KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.2204.04012

Keywords

Exo-beta-1,3-galactanase; glycoside hydrolase family 43; Penicillium oxalicum; larch wood arabinogalactans

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In this study, a novel exo-beta-1,3-galactanase named PoGal3 was identified and characterized. PoGal3 showed optimal activity at pH 5.0 and 40°C with beta-1,3-galactan as the preferred substrate. It also exhibited enhanced activity in the presence of Zn(2+). This enzyme has potential applications in the construction of glycan blocks for studying biological functions.
Arabinogalactans have diverse biological properties and can be used as pharmaceutical agents. Most arabinogalactans are composed of beta-(1 -> 3)-galactan, so it is particularly important to identify beta-1,3-galactanases that can selectively degrade them. In this study, a novel exo-beta-1,3-galactanase, named PoGal3, was screened from Penicillium oxalicum sp. 68, and hetero-expressed in P. pastoris GS115 as a soluble protein. PoGal3 belongs to glycoside hydrolase family 43 (GH43) and has a 1,356-bp gene length that encodes 451 amino acids residues. To study the enzymatic properties and substrate selectivity of PoGal3, beta-1,3-galactan (AG-P-I) from larch wood arabinogalactan (LWAG) was prepared and characterized by HPLC and NMR. Using AG-P-I as substrate, purified PoGal3 exhibited an optimal pH of 5.0 and temperature of 40 degrees C. We also discovered that Zn(2+)had the strongest promoting effect on enzyme activity, increasing it by 28.6%. Substrate specificity suggests that PoGal3 functions as an exo-beta-1,3-galactanase, with its greatest catalytic activity observed on AG-P-I. Hydrolytic products of AG-P-I are mainly composed of galactose and beta-1,6-galactobiose. In addition, PoGal3 can catalyze hydrolysis of LWAG to produce galacto-oligomers. PoGal3 is the first enzyme identified as an exo-beta-1,3-galactanase that can be used in building glycan blocks of crucial glycoconjugates to assess their biological functions.

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