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Colorimetric Quantification of β-(1→4)-Mannobiose and 4-O-β-D-Mannosyl-D-glucose

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Title: Colorimetric Quantification of β-(1→4)-Mannobiose and 4-O-β-D-Mannosyl-D-glucose
Authors: Jaito, Nongluck Browse this author
Saburi, Wataru Browse this author →KAKEN DB
Muto, Hirohiko Browse this author
Matsui, Hirokazu Browse this author →KAKEN DB
Mori, Haruhide Browse this author →KAKEN DB
Keywords: oligosaccharide quantification
cellobiose 2-epimerase
4-O-β-D-mannosyl-D-glucose phosphorylase
Issue Date: 20-Nov-2014
Publisher: 日本応用糖質科学会
Journal Title: Journal of Applied Glycoscience
Volume: 61
Issue: 4
Start Page: 117
End Page: 119
Publisher DOI: 10.5458/jag.jag.JAG-2014_007
Abstract: Spectrophotometric quantification method of carbohydrates is useful for processing multiple samples. In this study, we established colorimetric quantification for 4-O-β-D-mannosyl-D-glucose (Man-Glc) and β-(1→4)-mannobiose (Man2). For quantification of Man-Glc, phosphorolysis of Man-Glc catalyzed by 4-O-β-D-mannosyl-D-glucose phosphorylase (MGP) was coupled with quantification of D-glucose by the glucose oxidase-peroxidase method. In addition to MGP, cellobiose 2-epimerase (CE) was added for quantification of Man2. In both quantifications, a good linear relationship was obtained between A505 and the sample concentration (0-0.5 mM). The A505 values obtained at various concentrations of Man2 and Man-Glc were almost identical to those with equivalent D-glucose concentrations. Kinetic parameters of Ruminococcus albus and Rhodothermus marinus CEs for the epimerization of Man2 were determined using the quantification method for Man-Glc. Both enzymes showed 5-15-fold higher kcat/Km values than those for cellobiose and lactose, which supports the prediction that these enzymes utilize Man2 as a substrate in the β-mannan metabolic pathway.
Type: article (author version)
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 佐分利 亘

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