Biochemical characterization and key catalytic residue identification of a novel alpha-agarase with CBM2 domain.

ABSTRACT: Agarooligosaccharides have great potential in food industry because of their various bio-activities, while the limited availability and diversity of α-agarases hinder agarooligosaccharides' broader application. To overcome this limitation, a computer-assisted method was used to screen and identify novel agarases. Firstly, one novel α-agarase, AgaB, with an N-terminal CBM2 domain (the first report of this domain in agarases), was discovered. Purified agarases only exhibited activity against agarose, with optimum activity at 40℃ and pH 8.0. Analysis of hydrolysis products indicated that AgaB is an endo-type α-agarase, producing agarotetraose and agarohexaose. Secondly, AgaB truncated CBM2 showed increased K_m values, suggesting that CBM2 aids in substrate bindi

SUBMITTER: Yuan D 

PROVIDER: S-EPMC10740060 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature