4.7 Article

Gelation properties of salt-extracted pea protein induced by heat treatment

Journal

FOOD RESEARCH INTERNATIONAL
Volume 43, Issue 2, Pages 509-515

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.foodres.2009.09.039

Keywords

Pea protein isolate; Salt extracted; Soy protein isolate; Gelation; Gelling point; Minimum gelation concentration; Heating and cooling rate

Funding

  1. Natural Sciences and Engineering Research Council of Canada (NSERC)

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Gelation is one of the most important properties of plant proteins. In this paper, a low denaturation salt extraction method was used to extract pea (Pisum sativum L.) protein isolate from commercial pea flour. The gelation properties of this isolate were examined and compared to commercial products. The pea protein isolate followed the three-step process of gelation that is generally accepted for heat-induced gelation of globular proteins. The minimum gelation concentration of salt-extracted pea protein isolate (PPIs) was 5.5% while that of commercial pea protein isolate (PPIc) was 14.5%. The gelling point was in the range of 82-86 degrees C for 14.5% PPIs, 0.3 M NaCl at natural pH (5.65). With increasing heating rate, the gelling point tended to increase. Higher heating and cooling rates resulted in decreased final G' (storage modulus) and G '' (loss modulus) values, indicative of decreased gel strength. A higher protein concentration resulted in higher G' and G '' values and it Was found that there was a power law relationship between protein concentration and G' and G ''. Tan delta (delta) values decreased with increasing protein concentration and at concentrations of 5.5% and above, tan delta remained constant which means the critical concentration for gel formation was 5.5%. The values Of G' and G '' for Pills were greater than those of PPIc, and tan delta of PPIs was smaller, indicative of a stronger gel network. DSC data showed that PPIc had undergone denaturation whereas PPIs had not (Delta H = 15.81 J/g protein). Although rheometer data showed that the final G' value of commercial soy protein isolate (SPIc) was smaller than that of Pills, the gel prepared with SPIc was visually stronger than that of PPIs. The rheological data obtained with small amplitude oscillatory testing was not consistent with the actual observations. Overall, the low degree of denaturation of the PPIs resulted in a stronger gel than that of PPIc making the Pills a more attractive food ingredient. (C) 2009 Elsevier Ltd. All rights reserved.

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