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Am. J. Enol. Vitic. 42:2:123-127 (1991)
Copyright © 1991 by the American Society for Enology and Viticulture.
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Heat Haze Characteristics of Fractionated Wine Proteins

E. J. Waters 1, W. Wallace 2, and P. J. Williams 1

1 The Australian Wine Research Institute, Glen Osmond 5064, South Australia
2 Department of Agricultural Biochemistry, Waite Agricultural Research Institute, University of Adelaide, Glen Osmond, 5064, South Australia.

The proteins of a heat-unstable wine were fractionated by a combination of salting out with (NH4)2SO4 and ultrafiltration. The protein composition of the fractions, as observed by electrophoresis, and to a lesser extent by amino acid content, was distinct. The least soluble fraction [A, precipitated with 60% saturation of (NH4)2SO4] was dominated by a protein band of Mr 32 000, the fraction salted out with 65% to 70% saturation of (NH4)2SO4 [B] had a major protein of Mr 24 000, and the most soluble material [C, supernatant at 70% saturation of (NH4)2SO4] comprised proteins of Mr 26 000 and 24 000 [E] together with a carbohydrate-rich fraction [D]. The Coomassie dye-binding assay was unsuitable for protein quantification of the fractions because it underestimated the true values by 50% to 80%. A micro heat test applied to the fractions showed that the carbohydraterich component [D] was the most thermo-stable and apparently extended this stabilizing effect to the protein components [E] in the original isolate [C]. Fractions B and E gave the most haze with heat.

Key words: protein, haze, ammonium sulfate fractionation, dye-binding assay, heat test

Submitted on May 16, 1990




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Copyright © 1991 by the American Society for Enology and Viticulture.