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Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11

Paper ID Volume ID Publish Year Pages File Format Full-Text
35616 45098 2010 7 PDF Available
Title
Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11
Abstract

Intermolecular transglucosylation of cyclodextrin glycosyltransferase (CGTase) was investigated for its use in oligosaccharide synthesis. From the kinetic parameters of the CGTase-catalyzed transglucosylation reaction, using β-cyclodextrin (β-CD) as the glucosyl donor and various saccharides or derivatives as acceptors, the efficient acceptors of the Paenibacillus sp. A11 enzyme were glucose, sorbose, lactose and cellobiose. Amongst these acceptors, cellobiose showed the highest kcat/Km value. The transglucosylation yields of the reactions for cellobiose, sorbose and glucose acceptors were 78, 57 and 54%, respectively, making cellobiose the most efficient acceptor of the tested saccharides in coupling with β-CD. The optimal condition for the coupling reaction was determined as: 2% (w/v) β-CD and 0.5% (w/v) cellobiose, incubated with 64 U/mL of CGTase at 30 °C for 2 h. Two main transfer products detected by HPLC, PC1 and PC2, with retention times of 3.81 and 4.42 min, respectively, and a product ratio of 3:1, had a molecular mass of 504 and 666 Da, respectively, as analyzed by mass spectrometry. The structures suggested by NMR were a trisaccharide and a novel tetrasaccharide-containing cellobiose of the structures glc (α1 → 4) glc (β1 → 4) glc and glc (α1 → 4) glc (α1 → 4) glc (β1 → 4) glc, respectively. The products were found to be resistant to hydrolysis by α-amylase.

Keywords
Acceptor; Cyclodextrin glycosyltransferase (CGTase); Glucosyl donor; Oligosaccharides; Paenibacillus; Transglucosylation
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Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 45, Issue 6, June 2010, Pages 947–953
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us