PURIFICATION AND PROPERTIES OF A β-D-MANNOSIDE MANNOHYDROLASE FROM GUAR

Article abstract of DOI:10.1016/S0008-6215(00)80796-X

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.