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

被引：36

作者：

Akkermans, Cynthia ^{[1
,2
]}

Venema, Paul ^{[2
]}

van der Goot, Atze Jan ^{[1
]}

Boom, Remko M. ^{[1
]}

van der Linden, Erik ^{[2
]}

机构：

[1] Wageningen Univ, Food Engn Grp, NL-6700 EV Wageningen, Netherlands

[2] Wageningen Univ, Food Phys Grp, NL-6700 EV Wageningen, Netherlands

来源：

FOOD BIOPHYSICS | 2008年 / 3卷 / 04期

关键词：

beta-Lactoglobulin; Fibrils; Aggregation; Enzymatic hydrolysis; Peptide;

D O I：

10.1007/s11483-008-9094-3

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

This paper describes a low temperature, enzymatic route to induce fibrillar structures in a protein solution. The route comprises two steps. First, beta-lactoglobulin was hydrolyzed into peptides at pH 8 and 37 degrees 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.

引用

页码：390 / 394

页数：5

共 15 条

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