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• W1930219349 endingPage "429" @default.
• W1930219349 startingPage "421" @default.
• W1930219349 abstract "Immobilized keratinase can improve stability while retaining its proteolytic and keratinolytic properties. Conventional purification followed by chemical immobilization is a laborious and costly process. A new genetic construct was developed to produce the keratinase-streptavidin fusion protein. Consequently, the purification and immobilization of the fusion protein onto a biotinylated matrix can be accomplished in a single step. The method was tested in both the Bacillus subtilis and Escherichia coli systems. In B. subtilis, the fusion protein was produced extracellularly and readily immobilized from the medium. In E. coli, the fusion protein was produced intracellularly in inclusion bodies; additional separation and renaturation processes were required prior to immobilization from the cell extract. The overall efficiencies were approximately the same, 24-28%, using both systems." @default.
• W1930219349 created "2016-06-24" @default.
• W1930219349 creator A5044060660 @default.
• W1930219349 creator A5055299742 @default.
• W1930219349 creator A5067026339 @default.
• W1930219349 date "2002-12-18" @default.
• W1930219349 modified "2023-10-14" @default.
• W1930219349 title "Bioimmobilization of keratinase usingBacillus subtilis andEscherichia coli systems" @default.
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• W1930219349 doi "https://doi.org/10.1002/bit.10485" @default.
• W1930219349 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12491527" @default.
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