Date of Award

2013

Degree Type

Thesis

Degree Name

Master of Arts (MA)

Department

Food Science

Committee Chair

Mario Ferruzzi

Committee Member 1

Owen Jones

Committee Member 2

Jean-Christophe Rochet

Committee Member 3

Bill Aimutis

Abstract

While information regarding the impact of flavan-3-ol-protein interactions on food quality attributes (flavor, texture, and physical stability) exists, insight into the potential consequence of these interactions on bioavailability of health-promoting flavan-3-ols remains unclear. The ability of nonspecific protein interactions in flavan-3-ol rich foods and beverages to alter digestive stability and/or digestive release (bioaccessibility) of flavan-3-ols has been previously proposed but unconfirmed. The primary objective of this study was to characterize effects of individual milk proteins and the milk matrix on in vitro bioaccessibility of green tea flavan-3-ols from model beverage systems. As a secondary objective, the impact of protein gastrointestinal digestion on protein-flavan-3-ol binding was assessed using fluorometry. Protein solutions containing sodium-caseinate (S-CSN), α-lactalbumin (α-LA), β-lactoglobulin (β-LG) (0.356 mg/100 mL, 0.01 mg/100 mL, 0.035 mg/100 mL, respectively), or non-fat dry milk (NFDM, 0.1 mg/mL) were prepared in Jenness Koops buffer containing milk salts or dd water and formulated at dosages of 10, 20, and 40% (v/v) into model green tea beverages containing 60 mg/100 mL total flavan-3-ols. Samples were then subjected to in vitro digestion simulating

human gastric and small intestinal conditions. Pre- and post-digestion flavan-3-ol profiles were assessed by HPLC and relative (%) and absolute (μmol/g) bioaccessibility of individual flavan-3-ols were calculated. With regards to green tea beverages formulated to 40% with milk protein solutions, inclusion of S-CSN significantly decreased (p0.05) were observed at protein and JK levels tested. SDS-PAGE results demonstrated only partial digestion of protein after peptic digestion, and degradation of proteins toEGCG, the main flavan-3-ol in green tea, occurs when protein is partially digested by pepsin in the gastric phase. Further digestion by pancreatin in the small intestinal phase appeared to reduce capacity for binding. Combined these data suggest that interactions between individual milk proteins and flavan-3-ols may alter bioaccessibility. However, the extent of these effects is subtle and dependent on the ability of individual interactions to survive normal digestive conditions. Interestingly, salts typically found in milk serum may exert protective effects on polyphenols from tea, stabilizing them to digestive reactions that may lead to their degradation.

Included in

Food Science Commons

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