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Biochemical properties of a native ?-1,4-mannanase from Aspergillus aculeatus QH1 and partial characterization of its N-glycosylation.


ABSTRACT: N-glycosylation plays critical roles in protein secretion, sorting, stability, activity modulation, and interactions to other molecules in the eukaryotic organisms. Fungal ?-1,4-mannanases have been widely used in the agri-food industry and contribute to the pathogenesis on plants. However, the information on N-glycosylation of a specific fungal carbohydrate-active enzyme (CAZyme) is currently limited. Herein, a cDNA was cloned from Aspergillus aculeatus QH1, displaying a full length of 1302 bp with an open reading frame of 1134 bp encoding for a GH5 subfamily 7 ?-1, 4-mannanase, namely AacMan5_7A. The enzyme was purified and exhibited an optimal activity at pH 4.6 and 60 °C, hydrolyzing glucomannan and galactomannan, but not yeast mannan. AacMan5_7A is an N-glycosylated protein decorated with a high-mannose type glycan. Further through UPLC-ESI-MS/MS analysis, one of the four predicted N-glycosylation sites at N255 position was experimentally verified. The present study expands the information of N-glycosylation in fungal CAZymes, providing scientific bases for enhancing the production of fungal enzymes and their applications in food, feed, and plant biomass conversions.

SUBMITTER: Ma L 

PROVIDER: S-EPMC7887645 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

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Biochemical properties of a native β-1,4-mannanase from <i>Aspergillus aculeatus</i> QH1 and partial characterization of its N-glycosylation.

Ma Liqing L   Jiang Heping H   Li Weihua W   Qin Hua H   Lv Zhi Z   Huang Jiujiu J   Hou Xuewen X   Wang Weijun W  

Biochemistry and biophysics reports 20210212


N-glycosylation plays critical roles in protein secretion, sorting, stability, activity modulation, and interactions to other molecules in the eukaryotic organisms. Fungal β-1,4-mannanases have been widely used in the agri-food industry and contribute to the pathogenesis on plants. However, the information on N-glycosylation of a specific fungal carbohydrate-active enzyme (CAZyme) is currently limited. Herein, a cDNA was cloned from <i>Aspergillus aculeatus</i> QH1, displaying a full length of 1  ...[more]

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