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Optical techniques to determine thermal effects on proteins
Author(s) -
Kongraksawech Teepakorn,
VázquezLandaverde Pedro,
RodrigoGarcia Joaquín,
Torres José A.,
HuertaRuelas Jorge
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.1365-2621.2008.01794.x
Subject(s) - ionic strength , differential scanning calorimetry , sorbitol , bovine serum albumin , chemistry , denaturation (fissile materials) , optical rotation , thermal stability , repeatability , analytical chemistry (journal) , trehalose , chromatography , aqueous solution , biochemistry , nuclear chemistry , thermodynamics , organic chemistry , physics
Summary Optical rotation (OR) and transmitted light (TL) measurements were conducted on 1%, 2.5% and 5% (w/v) bovine serum albumin (BSA) in 0.01 m phosphate buffer at pH 7 and ionic strength 0.08. Denaturation temperatures ( T d ) obtained from OR measurements were consistent with reported differential scanning calorimetry values. Protein concentration did not affect T d in agreement with most reports. Changes in TL reflecting gel formation and protein aggregation were influenced by BSA concentration. Sugar concentration in the range used in this study (0–5%) did not affect the thermal stability of BSA. The lack of difference in sucrose, trehalose and sorbitol effects on the thermal stability of BSA was consistent with some but not all reports. The optical system used to study protein denaturation had acceptable accuracy (consistency with published T d values) and precision (coefficient of variation under 3.5%) levels.