Literature DB >> 14561134

Direct screening of libraries of yeast clones for alpha-amylase activity on raw starch hydrolysis.

Dominic W S Wong1, Sarah B Batt, Charles C Lee, George H Robertson.   

Abstract

High-throughput screening for high-activity barley alpha-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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Year:  2003        PMID: 14561134     DOI: 10.2174/0929866033478744

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  3 in total

1.  Enzyme-coupled assay for beta-xylosidase hydrolysis of natural substrates.

Authors:  Kurt Wagschal; Diana Franqui-Espiet; Charles C Lee; George H Robertson; Dominic W S Wong
Journal:  Appl Environ Microbiol       Date:  2005-09       Impact factor: 4.792

2.  Synergistic action of recombinant alpha-amylase and glucoamylase on the hydrolysis of starch granules.

Authors:  D W S Wong; G H Robertson; C C Lee; K Wagschal
Journal:  Protein J       Date:  2007-04       Impact factor: 4.000

3.  Characterization of active Lentinula edodes glucoamylase expressed and secreted by Saccharomyces cerevisiae.

Authors:  Dominic W S Wong; Sarah B Batt; Charles C Lee; Kurt Wagschal; George H Robertson
Journal:  Protein J       Date:  2005-11       Impact factor: 4.000

  3 in total

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