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Heat treatment of bovine alpha-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity.

Abstract:

Prolonged heating of holo bovine alpha-lactalbumin (BLA) at 80 degrees C in pH 7 phosphate buffer in the absence of a thiol initiator improves the surface activity of the protein at the air:water interface, as determined by surface tension measurements. Samples after 30, 60, and 120 min of heating were analyzed on cooling to room temperature. Size-exclusion chromatography shows sample heterogeneity that increases with the length of heating. After 120 min of heating monomeric, dimeric, and oli...

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Publication status:
Published

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Publisher copy:
10.1021/bi700897n

Authors


Wijesinha-Bettoni, R More by this author
Jenkins, JA More by this author
Mackie, AR More by this author
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Journal:
Biochemistry
Volume:
46
Issue:
34
Pages:
9774-9784
Publication date:
2007-08-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:1a9820d4-6bea-40f1-9c8f-cff807d33df0
Source identifiers:
33936
Local pid:
pubs:33936

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