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Beta -Amylase Activity and Thermostability in Two Mutants Derived from the Malting Barley cv. Triumph

Author: Swanston J.S.   Molina-Cano J-L.  

Publisher: Academic Press

ISSN: 0733-5210

Source: Journal of Cereal Science, Vol.33, Iss.2, 2001-03, pp. : 155-161

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Abstract

The malting barley cultivar, Triumph, and two mutants derived from it with higher (TL9) and lower (TL43) dormancy, respectively, were grown in replicated trials at Lleida, Spain and Dundee, Scotland, in 1999. Measurement ofbeta -amylase in the mature grain showed both mutants to have higher enzyme activity than the parental type with Spanish-grown samples higher in beta -amylase than Scottish-grown. There were no genotypic differences in beta-amylase thermostability or in the portion of the enzyme that was water-soluble. However, for all three genotypes, Scottish-grown samples had a higher proportion of water-soluble beta -amylase and total beta -amylase thermostability was also higher in the Scottish-grown samples. Data from the Spanish-grown samples suggested that water-soluble beta -amylase was slightly more thermostable than the portion of the enzyme released by papain.

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