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Dynamics of Evening Primrose Protein Hydrolysis

J. Golabczak, J. Strakowska, and A. Konstantynowicz

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

 

E-mail: jgolab@mail.p.lodz.pl

Abstract: Evening primrose protein isolate prepared by proteolysis was digested with trypsin at pH 8 and 50oC. Effects of enzyme and substrate concentrations and of digestion time on the degree of protein hydrolysis were determined. Experimental results were used to develop a mathematical model describing the path of enzymatic cleavage of evening primrose protein. According to this model, the process starts with the peptide bond hydrolysis followed either by formation of a stable enzymesubstrate complex or the peptide bond resynthesis, at the constant initial enzyme to substrate concentration ratio (ρ(E)0/ρ(S)0) and evening primrose protein concentrations of 20 to 50 g dm−3. Optimum proteolysis conditions (ρ(S)0 = 20 g dm−3, ρ(E)0/ρ(S)0 = 2 %, 5 h) provided the highest degree of protein hydrolysis of 28—30 %. Enzymatic digestion enhanced the content of low relative molar mass of peptides (easily absorbable in small intestine) in evening primrose protein hydrolyzate and increased its solubility in water.

Full paper in Portable Document Format: 596aa409.pdf

 

Chemical Papers 59 (6a) 409–412 (2005)

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