Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase

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...

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Veröffentlicht in:Food biophysics 2008-12, Vol.3 (4), p.390-394
Hauptverfasser: Akkermans, Cynthia, Venema, Paul, van der Goot, Atze Jan, Boom, Remko M, van der Linden, Erik
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Sprache:eng
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Zusammenfassung: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.
ISSN:1557-1858
1557-1866
DOI:10.1007/s11483-008-9094-3