4.7 Article

Sequential preheating and transglutaminase pretreatments improve stability of whey protein isolate at pH 7.0 during thermal sterilization

Journal

FOOD HYDROCOLLOIDS
Volume 31, Issue 2, Pages 306-316

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2012.11.018

Keywords

Whey protein; Transglutaminase; Thermal pretreatment; Sterilization; Transparency

Funding

  1. University of Tennessee
  2. Dairy Research Institute

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Whey protein isolate (WPI) is a potential ingredient to manufacture shelf-stable transparent beverages if proteins are heat stable, i.e., without causing turbidity, precipitation and gelation after the required thermal processing to obtain commercial sterility (138 degrees C for 8 s or longer). However, information is lacking about stability of WPI during heating at 138 degrees C. Furthermore, novel technology and mechanistic understanding on how to produce clear products after heating systems with >5% WPI, particularly with salt, is needed. In this work, 5% w/v WPI was pretreated by microbial transglutaminase (mTGase) at three levels for 1-15 h at 50 degrees C, with and without prior preheating at 80 degrees C for 15 min. Heat stability of the pretreated samples at pH 7.0 and 0, 50, and 100 mM NaCl was evaluated at 138 degrees C. Samples pretreated by mTGase for a greater extent demonstrated improved heat stability. Samples subjected to sequential preheating and mTGase pretreatments produced clear dispersions even after heating at 138 degrees C for 30 min in the presence of 0 and 50 mM NaCl at pH 7. All pretreatments increased the magnitude of zeta-potential and resistance against thermal denaturation. The sequentially-pretreated WPI was the most heat-resistant, having decreased hydrodynamic diameter (<36 nm) during extended heating at 138 degrees C and 50 mM NaCl. The present study demonstrates the feasibility of using sequential preheating and mTGase pretreatments to develop sterilized beverage products with a high content (5% w/v) of whey protein and yet of transparent appearance at ambient temperatures. (C) 2012 Elsevier Ltd. All rights reserved.

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