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Modification of Proteins from Evening Primrose by Transgluteminase

J. Golabczak, J. Strakowska, and A. Stan

Institute of Technical Biochemistry, Faculty of Biotechnology and Food Sciences, Technical University of Lodz, PL-90 924 Lodz

 

E-mail: jgolab@p.lodz.pl

Received: 1 April 2004

Abstract: 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.

Full paper in Portable Document Format: 586a415.pdf

 

Chemical Papers 58 (6) 415–417 (2004)

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