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Cholecystokinin release by STC‐1 cells in response to differentially hydrolyzed soy protein
Author(s) -
Krul Elaine Susan,
Li Jia,
Napawan Nida,
Tulk Barry,
Butteiger Dustie N
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.330.8
Subject(s) - cholecystokinin , hydrolysate , chemistry , hydrolysis , enzymatic hydrolysis , peptide , soy protein , enzyme , biochemistry , bovine serum albumin , receptor
Cholecystokinin (CCK) is a satiety signal released by intestinal I‐cells in response to peptides and other macronutrients. The molecular mechanism of the CCK response is poorly understood. The objective of our research was to identify satiating soy peptide molecules derived from differential enzymatic hydrolyses. Soluble soy protein hydrolysates were generated with at least 9 different food processing enzymes and then added to enteroendocrine cells (STC‐1) at 2 mg/mL protein for 4 hours to screen for their ability to induce CCK release. Phorbol 12‐myristate 13‐acetate (PMA) (100 nM) and 2 mg/mL bovine serum albumin (BSA) were used as positive and basal controls, respectively. Most hydrolyzed soy proteins significantly induced CCK over basal levels while non‐hydrolyzed proteins did not. Select hydrolysates induced CCK by 117 ± 15.0%, 113 ± 19.7% and 99 ± 13.8% (mean ± SEM) versus the PMA control, respectively, indicating that signaling of CCK release was dependent on peptide sequence specificity. CCK release was also modulated by the degree of hydrolysis for each enzyme. In conclusion, specific soy peptides generated by enzyme hydrolysis under defined conditions induce CCK release. Characterizing the specific sequences involved will help us develop peptide hydrolysates with increased satiety‐inducing potential which would have utility as ingredients in food products designed for use in weight management.