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 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
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. |
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ISSN: | 1557-1858 1557-1866 |
DOI: | 10.1007/s11483-008-9094-3 |