4.7 Article

Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties

Journal

FOOD HYDROCOLLOIDS
Volume 25, Issue 5, Pages 887-897

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2010.08.013

Keywords

Soy protein isolates; Enzymatic hydrolysis; Extrusion pre-treatment; Protein modification; Emulsifying properties

Funding

  1. National Natural Science Foundation of China [20806030]
  2. National High-tech R&D Program (863 Program) of China [2006AA10326]
  3. China Scholarship Council

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Effects of combined extrusion pre-treatment and controlled enzymatic hydrolysis on the physicochemical properties and emulsifying properties of soy protein isolates (SPI) have been investigated. Results showed that extrusion pre-treatment caused a marked improvement in the accessibility of SPI to enzymatic hydrolysis, resulting in changes in degree of hydrolysis (DH), protein solubility (PS), surface hydrophobicity (H-0) and molecular weight distributions (MWD) for ESPIH (extrusion pre-treated SPI hydrolysates). It was observed that emulsion systems formed by control SPI or SPIH (SPI hydrolysates) (20% v/v oil, 1.6% w/v emulsifier, and pH 7.0) were unstable over a quiescent storage period of 21 days, due to bridging flocculation and creaming. However, ESPIH (9.1% DH) was capable of producing a very fine emulsion (d(32) = 0.42 mu m, d(43) = 2.01 mu m) which remained stable over a long term quiescent storage. Various surface properties of ESPIH products have also been studied in relation to DH and emulsifying functionalities. It was suggested that significantly increased protein solubility and decreased molecular weight could be the main reasons for the greatly improved emulsifying capability of ESPIH. This study demonstrated that modified soy protein could be an excellent emulsifying agent for food and other applications. It also demonstrated that combined extrusion pre-treatment and enzymatic hydrolysis could be a highly effective method for functionality modification of globular proteins. (C) 2010 Elsevier Ltd. All rights reserved.

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