作者: Sissel Løkra , Reidar Barfod Schüller , Bjørg Egelandsdal , Bjørn Engebretsen , Knut Olav Strætkvern
DOI: 10.1016/J.LWT.2008.11.011
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摘要: Abstract Protein concentrates prepared by expanded bed adsorption (EBA) chromatography from industrial potato juice (PJ) were analysed for chemical composition, color, enzyme activities, thermal properties and selected functional (solubility emulsifying stability). Two EBA multi-modal resins, MIMO I-45 1300 (UpFront Chromatography), employed under various pH conditions resulting in four protein concentrates, A–D. Concentrate B contained an electrophoretically pure protease inhibitor fraction (20–21 kDa), whereas concentrate A, C D both patatin (41 kDa) inhibitors. The explored the presence of transitions native to denatured states using differential scanning calorimetry (DSC). had lower heat transition (Δ H ) T -onset than other concentrates. containing inhibitors exhibited highest denaturation temperature enthalpy. All differed significantly ( P