Expression and characterization of α-1,3-glucanase from Paenibacillus alginolyticus NBRC15375, which is classified into subgroup 2 (minor group) of GH family 87.

Autor:	Konishi Y; Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan.; Department of Food and Nutrition, Kyoto Bunkyo Junior College, Uji, Kyoto, Japan., Sato K; Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan., Nabetani K; Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan., Shirasaka N; Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan., Fukuta Y; Department of Applied Biological Chemistry, Faculty of Agriculture, Kindai University, Nara, Japan.
Jazyk:	angličtina
Zdroj:	Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2024 Apr 22; Vol. 88 (5), pp. 538-545.
DOI:	10.1093/bbb/zbae014
Abstrakt:	Bacterial α-1,3-glucanase, classified as glycoside hydrolase (GH) family 87, has been divided into 3 subgroups based on differences in gene sequences in the catalytic domain. The enzymatic properties of subgroups 1 and 3 of several bacteria have been previously investigated and reported; however, the chemical characterization of subgroup 2 enzymes has not been previously conducted. The α-1,3-glucanase gene from Paenibacillus alginolyticus NBRC15375 (PaAgl) belonging to subgroup 2 of GH family 87 was cloned and expressed in Escherichia coli. PgAgl-N1 (subgroup 3) and PgAgl-N2 (subgroup 1) from P. glycanilyticus NBRC16188 were expressed in E. coli, and their enzymatic characteristics were compared. The amino acid sequence of PaAgl demonstrated that the homology was significantly lower in other subgroups when only the catalytic domain was compared. The oligosaccharide products of the mutan-degrading reaction seemed to have different characteristics among subgroups 1, 2, and 3 in GH family 87. (© The Author(s) 2024. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.)
Databáze:	MEDLINE
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