Characterization of a Maltase from an Early-Diverged Non-Conventional Yeast Blastobotrys adeninivorans.

ABSTRACT: Genome of an early-diverged yeast Blastobotrys (Arxula) adeninivorans (Ba) encodes 88 glycoside hydrolases (GHs) including two α-glucosidases of GH13 family. One of those, the rna_ARAD1D20130g-encoded protein (BaAG2; 581 aa) was overexpressed in Escherichia coli, purified and characterized. We showed that maltose, other maltose-like substrates (maltulose, turanose, maltotriose, melezitose, malto-oligosaccharides of DP 4‒7) and sucrose were hydrolyzed by BaAG2, whereas isomaltose and isomaltose-like substrates (palatinose, α-methylglucoside) were not, confirming that BaAG2 is a maltase. BaAG2 was competitively inhibited by a diabetes drug acarbose (K_i = 0.8 µM) and Tris (K_i = 70.5 µM). BaAG2 w

SUBMITTER: Visnapuu T 

PROVIDER: S-EPMC6981392 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature