4.7 Article

In Vitro Digestibility of α-Casozepine, a Benzodiazepine-like Peptide from Bovine Casein, and Biological Activity of Its Main Proteolytic Fragment

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 59, Issue 9, Pages 4464-4472

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf104089c

Keywords

alpha-casozepine; simulated digestion; milk peptides; alpha(s1)-casein; anxiety

Funding

  1. Region Lorraine
  2. Institut National de la Recherche Agronomique (INRA)

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alpha-Casozepine is a peptide, corresponding to the sequence 91-100 of the bovine alpha(s1)-casein, displaying anxiolytic activity in the rat. The alpha(s1)-casein tryptic hydrolysate containing this peptide decreases stress effects after oral administration in various species including man. Therefore, the stability of this peptide toward gastric and pancreatic proteases has been assessed by using pepsin, chymotrypsin/trypsin, Corolase PP, pepsin followed by chyrnotrypsin/trypsin or pepsin followed by Corolase PP. alpha-Casozepine was slowly degraded by chymotrypsin, much more sensitive to pepsin and Corolase PP but not completely destroyed after 4 h kinetics. The bonds in the region 91 to 95 of the alpha-casozepine were totally resistant to hydrolysis by all studied proteases. Surprisingly, a fragment, corresponding to the sequence 91-97 and found in all the hydrolysis media in significant amount, possessed an anxiolytic activity in three behavioral tests measuring this parameter. This peptide could participate in the in vivo activity of alpha-casozepine.

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