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Preliminary studies to determine the chaperoning properties of bovine casein and crystallin proteins at reducing beef muscle protein aggregation during heating
Author(s) -
Pulford David J.,
Frost Debbie F.,
Lomiwes Dominic D.,
Farouk Mustafa M.
Publication year - 2008
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2008.01821.x
Subject(s) - casein , crystallin , chaperone (clinical) , protein aggregation , chemistry , bovine serum albumin , sarcoplasm , denaturation (fissile materials) , biochemistry , heat shock protein , endoplasmic reticulum , biophysics , biology , medicine , pathology , gene , nuclear chemistry
Summary The ability of small heat shock proteins (sHSP) at preventing the aggregation and precipitation of unfolded and misfolded proteins because of changes in pH and temperature is widely recognised. The performance of sHSP from bovine lens extract at protecting sarcoplasmic proteins from heat induced denaturation and aggregation was compared with other chaperones including bovine serum albumin, α s ‐casein, β‐casein and a synthetic peptide based upon αA‐crystallin (AAC). Beef sarcoplasmic proteins were heated in the presence or absence of exogenous chaperone and the solubility, surface hydrophobicity and enzymatic activities of the sarcoplasmic proteins was determined. Lens extract prevented the aggregation of sarcoplasmic proteins, maintaining solubility and clarity up to 65 °C relative to 60 °C for β‐casein. By contrast, α s ‐ and β‐casein proteins protected the activity of endogenous enzymes at temperatures between 37 °C and 52 °C, unlike lens sHSP. Our findings support the addition of casein proteins as potential thermal stabilisers of meat proteins in food systems.