Plant Foods for Human Nutrition

, Volume 40, Issue 4, pp 233–242 | Cite as

Specific role of endopeptidases in modulating the nature of protein digestion products

  • Laurent Savoie
  • Ruth Charbonneau


The impact of various endopeptidases on the nature of protein digestion products was measured with the digestion cell technique. After a 30 min pepsin pre-digestion, casein and rapeseed concentrates were hydrolyzed with various amounts of pancreatin, trypsin and/or chymotrypsin. This hydrolysis was performed in a dialysis tube (molecular weight cut-off 1000) with continuous collection of the digested material. The addition of pure trypsin or chymotrypsin to pancreatin (Enzyme:Substrate 1∶25) did not change the digestibility of casein. Only a higher pancreatin level (Enzyme: Substrate 1∶12.5) increased the total protein digestibility without affecting the amino acid spectra. Rapeseed digestibility was markedly increased by the addition of pure trypsin to pancreatin. Lysine and arginine, target amino acids of trypsin, were favored at the expense of chymotrypsin and elastase target amino acids. Supplementation of pancreatin with, chymotrypsin enhanced rapeseed digestibility without affecting the relative amino acid digestibility. The impact of a higher pancreatin ratio (Enzyme: Substrate 1∶12.5) was similar to that of enriched pancreatin but the rate of amino acid release was modified. The differences between protein sources were mainly attributed to protein structure.

Key words

in vitro digestion rapeseed casein trypsin chymotrypsin pancreatin 


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Copyright information

© Kluwer Academic Publishers 1990

Authors and Affiliations

  • Laurent Savoie
    • 1
  • Ruth Charbonneau
    • 1
  1. 1.Département de nutrition humaine et de consommation, Faculté des Sciences de l'agriculture et de l'alimentationUniversité LavalQuébecCanada

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