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Purification and Characterization of Escherichia coli Sulfite Reductase and its Application in Surimi Processing
Author(s) -
Yin L.J.,
Lin H.Y.,
Jiang S.T.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb09587.x
Subject(s) - sulfite reductase , sulfite , chemistry , escherichia coli , fractionation , mackerel , reductase , chromatography , biochemistry , ammonium , ammonium sulfate , enzyme , biology , fish <actinopterygii> , organic chemistry , fishery , gene
The NADPH‐sulfite reductase from Escherichia coli was purified to electrophoretic homogeneity by ammonium sulfate fractionation, and DEAE Sephacel and Sephacryl S‐300 HR chromatography. The recovery and molecular weight were 31.7% and 119000, while the optimal pH and temperature for the activity were 7.7 and 25°C, respectively. It was strongly inhibited by PCMB, KCN, Hg 2+ , Fe 2+ , Fe 3+ , Ca 2+ , Co 2+ , and Cu 2+ , moderately by NEM, PMSF, IAA, Cd 2+ , Zn 2+ , Mn 2+ , and Ba 2+ . Addition of purified reductase significantly increased the reactive SH and gel strength of surimi prepared from frozen mackerel. The data suggest the high potential of microbial NADPH‐sulfite reductase in surimi processing using frozen fish or denatured muscle proteins as raw materials. Keywords: Escherichia coli , sulfite reductase, mackerel, purification, characterization