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Modification of Proteins from Evening Primrose by Transgluteminase
Golabczak, J., Strakowska, J. and Stan, A. Modification of Proteins from Evening Primrose by Transgluteminase Chemical Papers, Vol.58, No. 6, 2004, 415-417
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Document type:
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Článok z časopisu / Journal Article |
Collection:
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Chemical papers
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Attached Files |
Name |
Description |
MIMEType |
Size |
Downloads |
n586a415.pdf
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586a415.pdf |
application/pdf |
106.30KB |
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Author(s) |
Golabczak, J. Strakowska, J. Stan, A.
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Title |
Modification of Proteins from Evening Primrose by Transgluteminase
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Journal name |
Chemical Papers
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Publication date |
2004
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Year available |
2004
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Volume number |
58
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Issue number |
6
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ISSN |
0366-6352
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Start page |
415
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End page |
417
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Place of publication |
Poland
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Publisher |
Versita
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Collection year |
2004
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Language |
english
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Subject |
270000 Biological Sciences 270100 Biochemistry and Cell Biology 270800 Biotechnology
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Abstract/Summary |
Application of transglutaminase for improvement of biological properties of evening primrose (Oenothera paradoxa) proteins was investigated. Proteins were extracted from defatted plant seeds being the waste material in pharmaceutical industry. The analysis of amino acids content of this protein extract proved the lysine deficiency. In order to increase its content, transglutaminase of guinea pig liver was employed. Low-degree papain hydrolyzate (DH = 7 %) of the protein extract and L-lysinium monochloride were used as the substrates for this reaction. This process resulted in an increase of lysine content from 1.3 % to 4.2 %. Transglutaminase has appeared to be efficient tool for modification of amino acid content in proteins.
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