Comparison of composition, enzyme activity and selected functional properties of potato proteins isolated from potato juice with two different expanded bed resins

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• 作者：Sissel Lø ; kra ; Reidar Barfod Sch&#xfc ; ller ; Bjø ; rg Egel ; sdal ; Bjø ; rn Engebretsen ; Knut Olav Stræ ; tkvern
• 关键词：Potato protein ; Patatin ; Protease inhibitors ; Expanded bed adsorption ; Mixed modal resin ; Emulsion ; Single electrode capacitance probe (SeCaP)
• 刊名：Lebensmittel-Wissenschaft und -Technologie
• 出版年：2009
• 出版时间：May 2009
• 年：2009
• 卷：42
• 期：4
• 页码：906-913
• 全文大小：331 K

文摘

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 properties (solubility and emulsifying stability). Two EBA multi-modal resins, MIMO I-45 and MIMO 1300 (UpFront Chromatography), were employed under various pH conditions resulting in four potato protein concentrates, A–D. Concentrate B contained an electrophoretically pure protease inhibitor fraction (20–21 kDa), whereas concentrate A, C and D contained both patatin (41 kDa) and protease inhibitors. The potato protein concentrates were explored for the presence of transitions from native to denatured states using differential scanning calorimetry (DSC). Concentrate C had lower heat of transition (ΔH) and T-onset than the other concentrates. The concentrate containing protease inhibitors exhibited the highest denaturation temperature and enthalpy. All concentrates differed significantly (P < 0.05) in color brightness, with concentrate B and D emerging as the brightest. The solubility of the concentrates was evaluated at pH 6 and pH 4.5. All concentrates had lower solubility at pH 4.5 than at pH 6 (70–80 % ). The stability of emulsions (1 % protein, 20 % oil, 0.08 % xanthan gum) against creaming was analysed with a new method based on the Single electrode Capacitance Probe (SeCaP) technology. Small differences among concentrates were observed by the new SeCaP method.