A new role of family 32 carbohydrate binding module in alginate lyase from Vibrio natriegens SK42.001 in altering its catalytic activity, thermostability and product distribution

2021 ◽  
pp. 101112
Author(s):  
Qing Meng ◽  
Licheng Zhou ◽  
Hinawi A.M. Hassanin ◽  
Bo Jiang ◽  
Yongchuang Liu ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Alginate Lyase ◽  
Product Distribution ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

scholarly journals Elucidation of a Unique Pattern and the Role of Carbohydrate Binding Module of an Alginate Lyase

Marine Drugs ◽  
2019 ◽  
Vol 18 (1) ◽  
pp. 32 ◽  
Author(s):  
Fu Hu ◽  
Benwei Zhu ◽  
Qian Li ◽  
Heng Yin ◽  
Yun Sun ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Degradation Products ◽  
Alginate Lyase ◽  
Product Distribution ◽  
Industrial Applications ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Release Process ◽  
Alginate Oligosaccharides ◽  
Degradation Pattern

Alginate oligosaccharides with different degrees of polymerization (DPs) possess diverse physiological activities. Therefore, in recent years, increasing attention has been drawn to the use of enzymes for the preparation of alginate oligosaccharides for food and industrial applications. Previously, we identified and characterized a novel bifunctional alginate lyase Aly7A, which can specifically release trisaccharide from three different substrate types with a unique degradation pattern. Herein, we investigated its degradation pattern by modular truncation and molecular docking. The results suggested that Aly7A adopted a unique action mode towards different substrates with the substrate chain sliding into the binding pocket of the catalytic domain to position the next trisaccharide for cleavage. Deletion of the Aly7A carbohydrate binding module (CBM) domain resulted in a complex distribution of degradation products and no preference for trisaccharide formation, indicating that the CBM may act as a “controller” during the trisaccharide release process. This study further testifies CBM as a regulator of product distribution and provides new insights into well-defined generation of alginate oligosaccharides with associated CBMs.

Hydrolysis of softwood by Aspergillus mannanase: Role of a carbohydrate-binding module

2010 ◽  
Vol 148 (4) ◽  
pp. 163-170 ◽  
Author(s):  
Tuan Anh Pham ◽  
Jean Guy Berrin ◽  
Eric Record ◽  
Kim Anh To ◽  
Jean-Claude Sigoillot
Keyword(s):  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Hydrolysis Of

Clostridium thermocellumXyn10B Carbohydrate-Binding Module 22-2:  The Role of Conserved Amino Acids in Ligand Binding†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (31) ◽  
pp. 9167-9176 ◽  
Author(s):  
Hefang Xie ◽  
Harry J. Gilbert ◽  
Simon J. Charnock ◽  
Gideon J. Davies ◽  
Michael P. Williamson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ligand Binding ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Conserved Amino Acids

scholarly journals Impact of Module-X2 and Carbohydrate Binding Module-3 on the catalytic activity of associated glycoside hydrolases towards plant biomass

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Nandita Pasari ◽  
Nidhi Adlakha ◽  
Mayank Gupta ◽  
Zeenat Bashir ◽  
Girish H. Rajacharya ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Plant Biomass ◽  
Glycoside Hydrolases ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

The role of carbohydrate-binding module (CBM) repeat of a multimodular xylanase (XynX) from Clostridium thermocellum in cellulose and xylan binding

2010 ◽  
Vol 48 (6) ◽  
pp. 856-861 ◽  
Author(s):  
Thangaswamy Selvaraj ◽  
Sung Kyum Kim ◽  
Yong Ho Kim ◽  
Yu Seok Jeong ◽  
Yu-Jeong Kim ◽  
...  
Keyword(s):  
Clostridium Thermocellum ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module

scholarly journals Modular Glucuronoxylan-Specific Xylanase with a Family CBM35 Carbohydrate-Binding Module

2012 ◽  
Vol 78 (11) ◽  
pp. 3923-3931 ◽  
Author(s):  
Susana Valeria Valenzuela ◽  
Pilar Diaz ◽  
F. I. Javier Pastor
Keyword(s):  
Catalytic Activity ◽  
Kinetic Parameters ◽  
Glucuronic Acid ◽  
Specific Activity ◽  
Dimensional Structure ◽  
Titration Calorimetry ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module ◽  
Content Type ◽  
Catalytic Module

ABSTRACTXyn30D from the xylanolytic strainPaenibacillus barcinonensishas been identified and characterized. The enzyme shows a modular structure comprising a catalytic module family 30 (GH30) and a carbohydrate-binding module family 35 (CBM35). Like GH30 xylanases, recombinant Xyn30D efficiently hydrolyzed glucuronoxylans and methyl-glucuronic acid branched xylooligosaccharides but showed no catalytic activity on arabinose-substituted xylans. Kinetic parameters of Xyn30D were determined on beechwood xylan, showing aKmof 14.72 mg/ml and akcatvalue of 1,510 min−1. The multidomain structure of Xyn30D clearly distinguishes it from the GH30 xylanases characterized to date, which are single-domain enzymes. The modules of the enzyme were individually expressed in a recombinant host and characterized. The isolated GH30 catalytic module showed specific activity, mode of action on xylan, and kinetic parameters that were similar to those of the full-length enzyme. Computer modeling of the three-dimensional structure of Xyn30D showed that the catalytic module is comprised of a common (β/α)8barrel linked to a side-associated β-structure. Several derivatives of the catalytic module with decreasing deletions of this associated structure were constructed. None of them showed catalytic activity, indicating the importance of the side β-structure in the catalysis of Xyn30D. Binding properties of the isolated carbohydrate-binding module were analyzed by affinity gel electrophoresis, which showed that the CBM35 of the enzyme binds to soluble glucuronoxylans and arabinoxylans. Analysis by isothermal titration calorimetry showed that CBM35 binds to glucuronic acid and requires calcium ions for binding. Occurrence of a CBM35 in a glucuronoxylan-specific xylanase is a differential trait of the enzyme characterized.

scholarly journals Fusion of family 2b carbohydrate-binding module increases the catalytic activity of a xylanase fromThermotoga maritimato soluble xylan

FEBS Letters ◽  
2003 ◽  
Vol 549 (1-3) ◽  
pp. 147-151 ◽  
Author(s):  
Farooqahmed S. Kittur ◽  
Selanere L. Mangala ◽  
Ahmed Abu Rus’d ◽  
Motomitsu Kitaoka ◽  
Hiroshi Tsujibo ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Module
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