BMC Biotechnol 2017 06 19;17(1):53. Epub 2017 Jun 19.
Agriculture and Agri-Food Canada, London Research and Development Centre, London, Ontario, Canada.
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Cell Stress Chaperones 2016 May 10;21(3):477-84. Epub 2016 Feb 10.
Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
The extracellular α-amylase from the hyperthermophilic archaeum Pyrococcus furiosus (PFA) is extremely thermostable and of an industrial importance and interest. PFA aggregates and accumulates as insoluble inclusion bodies when expressed as a heterologous protein at a high level in Escherichia coli. In the present study, we investigated the roles of chaperones from P. Read More
Biochemistry 2002 May;41(19):6193-201
Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824, USA.
The hyperthermophilic archeon Pyrococcus furiosus produces an extracellular alpha-amylase that belongs to glycosyl hydrolases' family 13. This enzyme is more thermostable than its bacterial and archaeal homologues (e.g. Read More
J Ind Microbiol Biotechnol 2007 Mar 22;34(3):187-92. Epub 2006 Nov 22.
Shanghai Institutes for Biological Sciences, Chinese Academy of Science, 500 Caobao Road, 200233 Shanghai, China.
The gene encoding the Pyrococcus furiosus extracellular alpha-amylase (PFA) was amplified by PCR from P. furiosus genomic DNA and was highly expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL. The recombinant alpha-amylase was mainly expressed in the form of insoluble inclusion bodies. Read More
Sci Rep 2016 Feb 26;6:22229. Epub 2016 Feb 26.
Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China.
Extracellular α-amylase from Pyrococcus furiosus (PFA) shows great starch-processing potential for industrial application due to its thermostability, long half-life and optimal activity at low pH; however, it is difficult to produce in large quantities. In contrast, α-amylase from Bacillus amyloliquefaciens (BAA) can be produced in larger quantities, but shows lower stability at high temperatures and low pH. Here, we describe a BAA protein expression pattern-mimicking strategy to express PFA in B. Read More