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Published on: March 4, 2009
Purification and structural characterization of LTP1 polypeptides from beer
S Jégou1, J P Douliez, D Mollé
1Unité de Biochimie et Technologie des Protéines, INRA, BP 71627, 44316 Nantes Cedex 03, France.
Journal of Agricultural and Food Chemistry
|October 29, 2000
Summary
Barley lipid transfer proteins (LTPs) undergo chemical changes like glycation during brewing. These modifications, particularly to LTP1, affect their structure and contribute to foam formation in beer.
Area of Science:
- Food Chemistry
- Biochemistry
- Brewing Science
Background:
- Lipid transfer proteins (LTPs) are crucial in plant tissues.
- Barley LTPs are implicated in beer foam stability.
- Understanding LTP modifications during brewing is essential.
Purpose of the Study:
- To purify and characterize barley lipid transfer proteins (LTPs).
- To investigate chemical modifications of LTPs during the brewing process.
- To elucidate the role of modified LTPs in beer foam.
Main Methods:
- Purification of LTPs from barley seeds and beer.
- Amino acid composition analysis.
- Disulfide bond analysis.
- Maillard reaction product analysis (glycation).
- Circular dichroism spectroscopy.
Main Results:
- Two forms of LTPs (LTP1 and LTPb) were purified from barley.
- Barley LTPs in beer exhibit reduced disulfide bonds and glycation via Maillard reaction.
- Glycation is heterogeneous, with variable hexose units attached.
- Reduced and glycated LTP1 is structurally unfolded.
Conclusions:
- Barley LTPs undergo significant chemical modifications during malting and brewing.
- Glycation and disulfide bond alterations impact LTP structure.
- These modifications are fundamental to understanding LTPs' function as foam-promoting agents in beer.
