| Literature DB >> 7011404 |
E Ichishima, M Arai, Y Shigematsu, H Kumagai, R Sumida-Tanaka.
Abstract
An acidic alpha-D-mannosidase (alpha-D-mannoside mannohydrolase, EC 3.2.1.24) has been isolated from culture filtrate of Aspergillus saitoi. The extracellular alpha-mannosidase was homogeneous in polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 51 000 and the isoelectric point pH 4.5. The purified enzyme has a pH optimum of 5.0, a Km of 0.45 mM with baker's yeast mannan and has no activity towards p-nitrophenyl-alpha-D-mannoside. The mode of action of the enzyme has been studied with baker's yeast mannan and saké yeast mannan. The enzyme cleaves specifically the 1,2-alpha-linked side chain, producing free mannose.Entities:
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Year: 1981 PMID: 7011404 DOI: 10.1016/0005-2744(81)90248-5
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002