Enzyme-induced formation of β-lactoglobulin fibrils by AspN endoproteinase

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Abstract

This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein solution. The route comprises two steps. First, β-lactoglobulin was hydrolyzed into peptides at pH 8 and 37°C with the enzyme AspN endoproteinase, which resulted in the formation of random aggregates. After hydrolysis, the pH was lowered to 2. As a result, long fibrillar aggregates were formed which was observed using transmission electron microscopy and Thioflavin T fluorescence measurements. © 2008 The Author(s).

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Akkermans, C., Venema, P., Van Der Goot, A. J., Boom, R. M., & Van Der Linden, E. (2008). Enzyme-induced formation of β-lactoglobulin fibrils by AspN endoproteinase. Food Biophysics, 3(4), 390–394. https://doi.org/10.1007/s11483-008-9094-3

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