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

C. Akkermans; P. Venema; A.J. van der Goot; R.M. Boom; E. van der Linden

doi:10.1007/s11483-008-9094-3

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

C. Akkermans, P. Venema, A.J. van der Goot, R.M. Boom, E. van der Linden

Research output: Contribution to journal › Article › Academic › peer-review

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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, 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 language	English
Pages (from-to)	390-394
Journal	Food Biophysics
Volume	3
Issue number	4
DOIs	https://doi.org/10.1007/s11483-008-9094-3
Publication status	Published - 2008

Keywords

amyloid fibrils
thioflavin-t
aggregation
hydrolysis
peptides
proteins

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10.1007/s11483-008-9094-3

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title = "Enzyme-induced Formation of {\ss}-Lactoglobulin Fibrils by AspN Endoproteinase",

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.",

keywords = "amyloid fibrils, thioflavin-t, aggregation, hydrolysis, peptides, proteins",

author = "C. Akkermans and P. Venema and {van der Goot}, A.J. and R.M. Boom and {van der Linden}, E.",

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T1 - Enzyme-induced Formation of ß-Lactoglobulin Fibrils by AspN Endoproteinase

AU - Akkermans, C.

AU - Venema, P.

AU - van der Goot, A.J.

AU - Boom, R.M.

AU - van der Linden, E.

N1 - F905

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

KW - amyloid fibrils

KW - thioflavin-t

KW - aggregation

KW - hydrolysis

KW - peptides

KW - proteins

U2 - 10.1007/s11483-008-9094-3

DO - 10.1007/s11483-008-9094-3

M3 - Article

SN - 1557-1858

VL - 3

SP - 390

EP - 394

JO - Food Biophysics

JF - Food Biophysics

IS - 4

ER -

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

Abstract

Keywords

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