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© 2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.

Abstract

The recombinant PhNah20A showed optimum hydrolytic activity on GlcNAc β-1,4 and β-1,3 linkages in chitobiose (GlcNAc)2 and GlcNAc-1,3-β-Gal-1,4-β-Glc (LNT2), the core structure of a human milk oligosaccharide, at pH 6.0 and 50 °C. Interestingly PhNah20A catalyzed the formation of LNT2, the non-reducing trisaccharide β-Gal-1,4-β-Glc-1,1-β-GlcNAc, and in low amounts the β-1,2- or β-1,3-linked trisaccharide β-Gal-1,4(β-GlcNAc)-1,x-Glc by a transglycosylation of lactose using 2-methyl-(1,2-dideoxy-α-d-glucopyrano)-oxazoline (NAG-oxazoline) as the donor [2]. The peptidoglycan of bacterial cell walls is hydrolyzed by muramidases/lysozymes, a lysozyme glycoside hydrolase (GH) family 22 C-type, from the upper gastrointestinal tract of the folivorous bird Opisthocomus hoazin in the native form and various mutants were expressed in Aspergillus oryzae. The inhibitor acarbose, in form of a transglycosylation product, was bound in the active site in the amylases from T. elegans and C. farinosa. [...]a potential novel binding site in the C-terminal domain of the Cordyceps enzyme was identified, which might be part of a starch interaction site [12]. The addition of the thermostable double mutant (A17S and K268N) to C. thermocellum secretome in order to carry out the hydrolysis of microcrystalline cellulose at 70 °C drastically increased the soluble glucose yield compared to the activity of the secretome supplemented with the wild-type enzyme [13].

Details

Title
Carbohydrate-Active Enzymes: Structure, Activity, and Reaction Products
Author
Benini, Stefano  VIAFID ORCID Logo 
First page
2727
Publication year
2020
Publication date
2020
Publisher
MDPI AG
ISSN
16616596
e-ISSN
14220067
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2392124947
Copyright
© 2020. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.