Acceptor Specificity and Transfer Efficiency of a β-Glycosidase from the China White Jade Snail

Molluscs display a sophisticated N-glycan pattern on their proteins, which is, in terms of involved structural features, even more diverse than that of vertebrates. This review summarises the current knowledge of mollusc N-glycan structures, with a focus on the functional aspects of the corresponding glycoproteins. Furthermore, the potential of mollusc-derived biomolecules for medical applications is addressed, emphasising the importance of mollusc research.

Section: Enzymes Involved In N-glycan Biosynthesismentioning

confidence: 99%

Mollusc N-glycosylation: Structures, Functions and Perspectives

Staudacher

2021

“…The different types of glycosidases are classified using different systems. One is the specificity for the glycon structure of their substrates, although it can be very often relaxed [ 14 ]. Enzymes from different sources can hydrolyze different glycopyranosides, and this is the case for bovine liver β-galactosidase or Pyrococcus furiosus , Sulfolobus solfataricus and Agrobacterium sp.…”

Section: Glycosyl Hydrolases: Mechanisms Use In Synthesis and Rarmentioning

confidence: 99%

“…The enzymatic formation of the β- d -fucosides is also hardly described in the scientific literature, and it deserves to be mentioned here. Acceptor specificity for monosaccharides and transfer efficiency have both been investigated for a glycosidase isolated from the China white jade snail [ 14 ]. An extraordinarily broad substrate specificity for both hydrolysis and transglycosylation was exhibited by this biocatalyst, and from the results obtained, the authors indicated a very high transfucosylation efficiency using p-nitrophenyl β- d -fucopyranoside at 10 mM and various acceptors (at 20 to 100 mM), such as glucose (88% yield) and xylose (93% yield); the interglycosidic linkage formed with glucose was β-1,6; thus, they proposed this biocatalyst as a useful candidate for Fuc-β-Glc and Fuc-β-Xyl disaccharide synthesis.…”

Section: Fucosidasementioning

confidence: 99%

Uncommon Glycosidases for the Enzymatic Preparation of Glycosides

Trincone

2015

Most of the reports in literature dedicated to the use of glycosyl hydrolases for the preparation of glycosides are about gluco- (α- and β-form) and galacto-sidase (β-form), reflecting the high-availability of both anomers of glucosides and of β-galactosides and their wide-ranging applications. Hence, the idea of this review was to analyze the literature focusing on hardly-mentioned natural and engineered glycosyl hydrolases. Their performances in the synthetic mode and natural hydrolytic potential are examined. Both the choice of articles and their discussion are from a biomolecular and a biotechnological perspective of the biocatalytic process, shedding light on new applicative ideas and on the assortment of biomolecular diversity. The hope is to elicit new interest for the development of biocatalysis and to gather attention of biocatalyst practitioners for glycosynthesis.

“…An extraordinarily broad substrate specificity for both hydrolysis and transglycosylation was exhibited by a glycosidase isolated from the China white jade snail. Acceptor specificity for monosaccharides and transfer efficiency have both been investigated for this promising enzyme [27] and from the results obtained, the authors indicated a very high transfucosylation efficiency using p-nitrophenyl derivative of β-D-fucose at 10 mM and acceptors (at 20–100 mM) such as glucose (88% yield) and xylose (93% yield); the interglycosidic linkage formed with glucose is β-1,6 thus they proposed this biocatalyst as a useful candidate for disaccharide synthesis. The Fuc-β-Xyl disaccharide formed in other reactions is a building block for the synthesis of asterosaponins of marine origin, although in natural compound the interglycosidic linkage is different (Fuc-β-(1-2)-Xyl) [28].…”

Section: Natural Enzymes For the Synthesis Of Glycosidic Linkagesmentioning

confidence: 99%

Angling for Uniqueness in Enzymatic Preparation of Glycosides

Trincone

2013

In the early days of biocatalysis, limitations of an enzyme modeled the enzymatic applications; nowadays the enzyme can be engineered to be suitable for the process requirements. This is a general bird’s-eye view and as such cannot be specific for articulated situations found in different classes of enzymes or for selected enzymatic processes. As far as the enzymatic preparation of glycosides is concerned, recent scientific literature is awash with examples of uniqueness related to the features of the biocatalyst (yield, substrate specificity, regioselectivity, and resistance to a particular reaction condition). The invention of glycosynthases is just one of the aspects that has thrust forward the research in this field. Protein engineering, metagenomics and reaction engineering have led to the discovery of an expanding number of novel enzymes and to the setting up of new bio-based processes for the preparation of glycosides. In this review, new examples from the last decade are compiled with attention both to cases in which naturally present, as well as genetically inserted, characteristics of the catalysts make them attractive for biocatalysis.