Carbohydrate Research p. 75 - 92 (1982)
Update date:2022-08-05
Topics:
McClearly, Barry V.
A β-D-mannoside mannohydrolase enzyme has been purified to homogeneity from germinated guar-seeds.Difficulties associated with the extraction and purification appeared to be due to an interaction of the enzyme with other protein material.The purified enzyme hydrolysed various natural and synthetic substrates, including β-D-manno-oligosaccharides and reduced β-D-manno-oligosaccharides of degree of polymerisation 2 to 6, as well as p-nitrophenyl, naphthyl, and methylumbelliferyl β-D-mannopyranosides.The preferred, natural substrate was β-D-mannopentaose, which was hydrolysed at twice the rate of β-D-mannotetraose and five times the rate of β-D-mannotriose.This result, together with the observation that α-D-mannose is released on hydrolysis, indicates that the enzyme is an exo-β-D-mannanase.
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Doi:10.1007/BF00929034
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(1979)Doi:10.1002/chem.200305232
(2004)Doi:10.1039/b312716h
(2004)Doi:10.1021/jm00322a045
(1966)Doi:10.1055/s-2002-20969
(2002)
