Abstract
The producer of fungal penicillopepsin, an aspartate protease, has been created by genetic engineering. The biochemical and physicochemical properties of the penicillopepsin enzyme preparation obtained from the culture liquid of the producer were studied. Properties of the new enzyme preparation and the commercially available aspergillopepsin were compared. Their proteolytic activities were found to be 670-680 U/g of the preparation. The soluble protein yield upon the wheat flour hydrolysis with penicillopepsin was 2.7 times higher than with aspergillopepsin. It is probably caused by the presence of the xylanase activity in the penicillopepsin preparation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Aspartic Acid Endopeptidases / genetics
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Aspartic Acid Endopeptidases / metabolism*
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Aspartic Acid Proteases / genetics
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Aspartic Acid Proteases / metabolism*
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Endo-1,4-beta Xylanases / genetics
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Endo-1,4-beta Xylanases / metabolism
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Flour / analysis
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Gene Expression
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Genetic Engineering
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Hydrolysis
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Kinetics
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Molecular Sequence Data
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Penicillium / enzymology*
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Penicillium / genetics
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Plasmids / chemistry
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Plasmids / metabolism
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Proteolysis
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Triticum / metabolism
Substances
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Fungal Proteins
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Recombinant Proteins
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Endo-1,4-beta Xylanases
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Aspartic Acid Proteases
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Aspartic Acid Endopeptidases
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aspergillopepsin I