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Direct Screening Of Libraries Of Yeast Clones For α-Amylase Activity On Raw Starch Hydrolysis

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High-throughput screening for high-activity barley a-amylase mutants expressed in Saccharomyces cerevisiae is hampered by the interference of reducing agents, particularly the glucose used in yeast growth media. The present investigation employed colorimetric and chemiluminescent detection systems that enable direct and rapid screening of activities on raw starch substrate. Active clones could be separated into two groups, based on high total activity or high specific activity.
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Keywords: amy1; amylase; barley seed amylase; high-throughput assay; starch hydrolysis; yeast library

Document Type: Review Article

Affiliations: Western Regional Research Center, USDA-Agricultural Research Service, 800 Buchanan Street, Albany, CA

Publication date: 01 October 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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