Enzyme-induced Formation of ß-Lactoglobulin Fibrils by AspN Endoproteinase

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29 Citations (Scopus)

Abstract

This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein solution. The route comprises two steps. First, ß-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.
Original languageEnglish
Pages (from-to)390-394
JournalFood Biophysics
Volume3
Issue number4
DOIs
Publication statusPublished - 2008

Keywords

  • amyloid fibrils
  • thioflavin-t
  • aggregation
  • hydrolysis
  • peptides
  • proteins

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