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Related Experiment Video

Updated: Jun 24, 2026

Preparation of Homogeneous MALDI Samples for Quantitative Applications

Preparation of Homogeneous MALDI Samples for Quantitative Applications

Published on: October 28, 2016

Structural changes of malt proteins during boiling.

Bei Jin¹, Lin Li, Guo-Qin Liu

¹Department of Food Science and Technology, South China University of Technology, Guangzhou, PR China.

Molecules (Basel, Switzerland)

|March 24, 2009

Summary

This summary is machine-generated.

Wort boiling causes protein unfolding, altering beer quality independently of malt variety. Key changes include reduced hydrophobicity and increased random coil structures, with a stable 40 kDa protein remaining.

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Area of Science:

Food Science
Biochemistry
Brewing Science

Background:

Protein structure significantly impacts beer quality.
Understanding protein behavior during wort boiling is crucial for brewers.

Purpose of the Study:

To investigate protein structural changes during wort boiling.
To compare these changes between two malt varieties (Baudin and Guangmai).

Main Methods:

Differential scanning calorimetry (DSC)
SDS-PAGE and two-dimensional electrophoresis
Gel filtration chromatography and circular dichroism (CD) spectroscopy

Main Results:

Boiling caused gradual protein unfolding, indicated by decreased surface hydrophobicity, free sulfhydryl content, and enthalpy.
Alpha-helix content decreased, while random coil content increased.
A stable 40 kDa boiling-resistant protein was identified; soluble aggregates formed via hydrophobic interactions.

Conclusions:

Wort boiling induces protein structural changes, primarily unfolding.
These protein alterations are largely independent of the malt variety used.
Observed protein changes may influence final beer quality.