Structural characterization on a β-agarase Aga86A_Wa from Wenyingzhuangia aestuarii reveals the prevalent methyl-galactose accommodation capacity of GH86 enzymes at subsite −1-Reference-Cited by-同舟云学术

Structural characterization on a β-agarase Aga86A_Wa from Wenyingzhuangia aestuarii reveals the prevalent methyl-galactose accommodation capacity of GH86 enzymes at subsite −1

Published:2023-04 Issue: Volume:306 Page:120594
ISSN:0144-8617
Container-title:Carbohydrate Polymers
language:en
Short-container-title:Carbohydrate Polymers

Author:

Zhang Yuying,Dong Sheng,Chen Guangning,Cao Siqi,Shen Jingjing,Mei Xuanwei,Cui Qiu,Feng Yingang,Chang Yaoguang,Wang Yanchao,Xue Changhu

Publisher

Elsevier BV

Subject

Materials Chemistry,Polymers and Plastics,Organic Chemistry

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4. Expression and characterization of a methylated galactose-accommodating GH86 β-agarase from a marine bacterium;Cao;Journal of Agricultural and Food Chemistry,2020

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2. The characteristic structure of funoran could be hydrolyzed by a GH86 family enzyme (Aga86A_Wa): Discovery of the funoran hydrolase;Carbohydrate Polymers;2023-10

3. Three marine species of the genus Fulvivirga, rich sources of carbohydrate-active enzymes degrading alginate, chitin, laminarin, starch, and xylan;Scientific Reports;2023-04-18