Abstract
Extensive studies have been done on beta-lactoglobulin (beta-Lg) fibrils in the past decade due to their potential as functional food ingredients, gelling agents, and encapsulation devices etc. (van der Goot, A. J.; Peighambardoust, S. H.; Akkermans, C.; van Oosten-Manski, J. M. Creating novel structures in food materials: The role of well-defined shear flow. Food Biophys. 2008, 3(2), 120-125 and Loveday, S. M.; Rao, M. A.; Creamer, L. K.; Singh, H. Factors affecting rheological characteristics of fibril gels: The case of beta-lactoglobulin and alpha-lactalbumin. J. Food Sci. 2009, 74 (3), R47-R55). However, most of the studies focus on the formation and mechanism of the fibrils. Little is known about fibril digestibility to date. In this work, in vitro pepsin digestion of bovine beta-lactoglobulin (beta-Lg) fibrils in simulated gastric fluid was investigated using thioflavin T fluorescence photometry, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, size-exclusion chromatography, matrix-assisted laser desorption/ionization mass spectrometry, and transmission electron microscopy (TEM). The fibrils were formed by heating beta-Lg solutions at 80 degrees C and pH 2.0 for 20 h. The fibrils were found to be digested completely by pepsin within 2 min, when long, straight fibrils were no longer observed by TEM. The peptides in the fibrils (2000-8000 Da) could be digested to smaller peptides (mostly <2000 Da) by pepsin. The peptides in the fibrils were believed to be more susceptible for pepsin to access and attack because of their hydrophobic nature. For comparison purposes, solutions of beta-Lg heated at neutral pH (pH 7.4) were also studied under the same conditions.
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