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Unfermented and Fermented Cocoa Extracts as Inhibitors of Pancreatic α‐Amylase, α‐Glucosidase, and Pancreatic Lipase
Author(s) -
Ryan Caroline,
Ye Liyun,
O'Keefe Sean,
Neilson Andrew Peter
Publication year - 2016
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.30.1_supplement.691.30
Subject(s) - acarbose , chemistry , food science , lipase , amylase , fermentation , polyphenol , roasting , cocoa bean , biochemistry , enzyme , antioxidant
Fermentation and roasting of cocoa ( Theobroma cacao) decrease levels of flavan‐3‐ols, which may aid in prevention of obesity and type‐2 diabetes. Our objective was to determine the impact of fermentation and roasting on the ability of cocoa to inhibit digestive enzymes. Polyphenol profiles of unfermented bean (UB), fermented bean (FB), unfermented liquor (UL), and fermented liquor (FL) extracts were characterized by colorimetric and chromatographic methods. Inhibitory activities of the cocoa extracts against pancreatic α‐amylase, α‐glucosidase, and pancreatic lipase were measured in vitro . Overall, there was a significant decrease (p<0.05) in total polyphenols, flavan‐3‐ols, and anthocyanins between the two sets of unfermented and fermented cocoa samples. HPLC and thiolysis demonstrated a decrease in catechins between unfermented and fermented samples as well as an increase in average flavanol degree of polymerization from UB to FB. For α‐glucosidase, UL, FL, Acarbose (+ control), FB, and UB had IC 50 values of 90.0, 109, 158, 200, and 218 μg/mL, respectively. This is a novel finding that suggests the potential utility of cocoa, particularly that of cocoa liquors, in blunting increases of blood glucose similar to the drug Acarbose. For α‐amylase and pancreatic lipase, Acarbose and Orlistat (+ controls) had the lowest IC 50 values (54.3 and 181 μg/mL, respectively) compared to the cocoa samples. However, at 500 μg/mL concentrations, Acarbose, FB, and FL inhibited α‐amylase 71.0%, 53.6%, and 38.4% respectively, all of which were not significantly different (p<0.05). The same was true for inhibition of pancreatic lipase by Orlistat (62.9%), UB (47.6%), and FB (41.5%) at 200 μg/mL concentrations. Thus, at high concentrations, inhibition of fermented cocoa and Acarbose against α‐amylase and that of cocoa beans and Orlistat against lipase are similar. Although processing induced significant changes in the polyphenol profiles of these cocoas, each enzyme was affected differently by fermentation and roasting of the samples. For α‐glucosidase, roasting of cocoa improved its inhibitory activity. For α‐amylase, both fermentation and roasting decreased cocoa's inhibition abilities, whereas these processes improved its inhibition of pancreatic lipase. Inhibition of these enzymes delays the digestion of carbohydrates and lipids, potentially dallying or blunting increases in postprandial blood glucose levels, reducing fat accumulation, and increasing satiety. These results suggest that compositional changes in cocoa during processing, other than alterations to polyphenols, influence potential inhibition of digestive enzymes.