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Effect of protein denaturation on void fraction in foam separation column
Authors:Tanner  Robert D  Parker  Tobias  Ko  Samuel  Ding  Yuoing  Loha  Veara  Du  Liping  Prokop  Ales
Institution:(1) Chemical Engineering Department, Vanderbilt University, 24th and Garland Avenues, 37235 Nashville, TN;(2) Present address: King Mongkut's Institute of Technology, Thonburi, Thailand
Abstract:Foam fractionation is a cost-effective process that uses air to extract protein from a liquid (in this case “crude” dilute egg-albumin solution). This article deals with how the void fraction (fraction of air in the aerated solution) of foam is affected by heat denaturation of the protein. A 2-mm glass tube was used to sample the foam-liquid interface fluid in a 35-mm-diameter column in order to detect small changes in void fraction and foam production, which are not easily detected directly from the bulk foam. The main control variablein this study was the protein solution preheating time. As the preheating time increased, the initial void fraction in the column decreased. The initial void fraction of the undenatured solution ranged from about 0.73 to 0.80, and the void fraction for significant preheating times of 5 min ranged from approx 0.68 to 0.72. Furthermore, the period of foam production increased from 5 to 7 min for undenatured proteins in solution to as long 15 min for 5-min preheated solutions. Side-port sampling through a small capillary tube has the potential to be used as a rapid and inexpensive way to determine the level of protein denaturation by directly determining the void fraction and then estimating the effect of denaturation from a protein denaturation calibration curve of the void fraction.
Keywords:Egg albumin  protein denaturation  foam fractionation  hydrophobicity  void fraction
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