Results 161 to 170 of about 15,361 (204)
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Bifidobacterium glycoside hydrolases and (potential) prebiotics

Innovative Food Science & Emerging Technologies, 2008
Abstract Carbohydrates occur in food as natural constituents or are added as ingredients. In the last decade a number of novel dietary carbohydrates have been introduced as ingredients for food applications, responding to the growing awareness among consumers of the link between health and diet.
van den Broek, L.A.M., Voragen, A.G.J.
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Hierarchical classification of glycoside hydrolases

Biochemistry (Moscow), 2011
This review deals with structural and functional features of glycoside hydrolases, a widespread group of enzymes present in almost all living organisms. Their catalytic domains are grouped into 120 amino acid sequence-based families in the international classification of the carbohydrate-active enzymes (CAZy database).
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Bioprospecting Metagenomics for New Glycoside Hydrolases

2012
To efficiently deconstruct recalcitrant plant biomass to fermentable sugars in industrial processes, biocatalysts of higher performance and lower cost are required. The genetic diversity found in the metagenomes of natural microbial biomass decay communities may harbor such enzymes.
Safiyh Taghavi   +5 more
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Xylanases of glycoside hydrolase family 30 – An overview

Biotechnology Advances, 2021
Xylan is the most abundant hemicellulose in nature and as such it is a huge source of renewable carbon. Its bioconversion requires a battery of xylanolytic enzymes. Of them the most important are the endo-β-1,4-xylanases which depolymerize the polysaccharide into smaller fragments.
Vladimír Puchart   +2 more
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Physiological roles of plant glycoside hydrolases

Planta, 2007
The functions of plant glycoside hydrolases and transglycosidases have been studied using different biochemical and molecular genetic approaches. These enzymes are involved in the metabolism of various carbohydrates containing compounds present in the plant tissues. The structural and functional diversity of the carbohydrates implies a vast spectrum of
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Diversity of phosphorylases in glycoside hydrolase families

Applied Microbiology and Biotechnology, 2015
Phosphorylases are useful catalysts for the practical preparation of various sugars. The number of known specificities was 13 in 2002 and is now 30. The drastic increase in available genome sequences has facilitated the discovery of novel activities.
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Strategies for tailoring pH performances of glycoside hydrolases

Critical Reviews in Biotechnology, 2021
Glycoside hydrolases (GHs) exhibit high activity and stability under harsh conditions, such as high temperatures and extreme pHs, given their wide use in industrial biotechnology. However, strategies for improving the acidophilic and alkalophilic adaptations of GHs are poorly summarized due to the complexity of the mechanisms of these adaptations. This
Shu-Fang, Li   +3 more
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Family 4 glycoside hydrolases are special: The first β-elimination mechanism amongst glycoside hydrolases

Biocatalysis and Biotransformation, 2006
The glycoside hydrolases are a large group of enzymes that can be grouped into two major mechanistic classes based upon the stereochemical outcome of catalysis: retention and inversion of sugar anomeric configuration. Both mechanisms involve nucleophilic displacement at the anomeric center, and both proceed via positively charged oxocarbenium ion-like ...
Vivian L. Y. Yip, Stephen G. Withers
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Glycoside hydrolases of rumen bacteria and protozoa

Current Microbiology, 1984
Sixteen strains of rumen bacteria and 21 protozoal preparations were screened for glycoside hydrolase and phosphatase activity, using 22 nitrophenyl glycoside substrates. The range and level of bacterial enzyme activities were species dependent, although, the glycosidases associated with plant cell wall breakdown were most active in the cellulolytic ...
Alan G. Williams   +2 more
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Glycoside hydrolases: Catalytic base/nucleophile diversity

Biotechnology and Bioengineering, 2010
AbstractRecent studies have shown that a number of glycoside hydrolase families do not follow the classical catalytic mechanisms, as they lack a typical catalytic base/nucleophile. A variety of mechanisms are used to replace this function, including substrate‐assisted catalysis, a network of several residues, and the use of non‐carboxylate residues or ...
Thu V. Vuong, David Wilson
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