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Further purification and characterisation of a new amylase found in barley
Author(s) -
Macgregor Alexander W.,
Daussant Jean,
NikuPaavola MarjaL
Publication year - 1979
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740301109
Subject(s) - amylase , isoelectric point , chemistry , amylose , chromatography , enzyme , isoelectric focusing , ion chromatography , hordeum vulgare , biochemistry , biology , poaceae , starch , botany
An amylase, previously detected in barley and described as a new barley amylase, has been further purified by immuno‐affinity and ion exchange chromatography on CM‐cellulose Analysis by isoelectricfocusing and immunochemical techniques showed that thses enzyme preparation did not contain the normal α‐ and β‐amylases usually found barley and malt. The enzyme had a very low isoelectric point ( ca pH 3.0) and was identified as an α‐amylase on the basis of its action pattern on amylose.