Dynamics of Evening Primrose Protein Hydrolysis

Golabczak, J., Strakowska, J. and Konstantynowicz, A. Dynamics of Evening Primrose Protein Hydrolysis Chemical Papers, Vol.59, No. 6a, 2005, 409-412

Document type: Článok z časopisu / Journal Article
Collection: Chemical papers  
 
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Author(s) Golabczak, J.
Strakowska, J.
Konstantynowicz, A.
Title Dynamics of Evening Primrose Protein Hydrolysis
Journal name Chemical Papers
Publication date 2005
Year available 2005
Volume number 59
Issue number 6a
ISSN 0366-6352
Start page 409
End page 412
Place of publication Poland
Publisher Versita
Collection year 2005
Language english
Subject 270000 Biological Sciences
270100 Biochemistry and Cell Biology
Abstract/Summary 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.
 
 
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