Determination of specific activities of malt α-amylases
1992; Elsevier BV; Volume: 16; Issue: 3 Linguagem: Inglês
10.1016/s0733-5210(09)80089-1
ISSN1095-9963
Autores Tópico(s)Microbial Metabolites in Food Biotechnology
ResumoHighly purified samples of α-amylases 1 and 2 were prepared from malted barley using ion exchange chromatography on carboxymethyl cellulose and affinity chromatography on cyclohepta-amylose epoxy Sepharose 6B. Specific activities of the two enzymes on amylose were determined by using end-group analysis of the products formed. Per unit of protein, the specific activity of α-amylase 2 was 2·3 times higher than that of α-amylase 1.
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