Research Article

Gel-enhancing effect and protein cross- linking ability of tilapia sarcoplasmic proteins

  1. Jirawat Yongsawatdigul*,
  2. Penprabha Piyadhammaviboon

Article first published online: 5 OCT 2007

DOI: 10.1002/jsfa.2993

Issue

Journal of the Science of Food and Agriculture

Journal of the Science of Food and Agriculture

Volume 87, Issue 15, pages 2810–2816, December 2007

Additional Information

How to Cite

Yongsawatdigul, J. and Piyadhammaviboon, P. (2007), Gel-enhancing effect and protein cross- linking ability of tilapia sarcoplasmic proteins. J. Sci. Food Agric., 87: 2810–2816. doi: 10.1002/jsfa.2993

Author Information

  1. School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000 Thailand

*School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000 Thailand

Publication History

  1. Issue published online: 9 NOV 2007
  2. Article first published online: 5 OCT 2007
  3. Manuscript Accepted: 4 APR 2007
  4. Manuscript Revised: 29 MAR 2007
  5. Manuscript Received: 25 OCT 2006

Funded by

  • National Center for Genetic Engineering and Biotechnology (BIOTEC), Bangkok, Thailand. Grant Number: BT-B-06-FM-19-4404

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Keywords:

  • sarcoplasmic protein;
  • tilapia;
  • transglutaminase;
  • lizardfish surimi;
  • protein cross-linking

Abstract

BACKGROUND: Tilapia (Oreochromis niloticus) sarcoplasmic proteins contain substantial transglutaminase (TGase) activity. The enzyme catalyzes the protein cross-linking reaction, resulting in a more elastic gel. The objective was to investigate the gel-enhancing effect of sarcoplasmic proteins from tilapia as related to TGase activity.

RESULTS: Total TGase activity of sarcoplasmic proteins concentrate (SpC) increased about 3.6-fold after ultrafiltration using 30 kDa membrane, but specific activity remained unchanged, indicating minimal TGase purification by ultrafiltration. Addition of 1 mg mL−1 SpC containing 40 units TGase activity induced cross-linking of tilapia actomyosin, and the extent of cross-linking increased with added level of SpC. Myosin heavy chain (MHC) and troponin were preferably cross-linked by tilapia SpC, while actin and tropomyosin were not affected. Higher retention of MHC was observed concomitantly with greater content of cross-linked protein when SpC was added to lizardfish surimi. Lizardfish surimi with 10 g kg−1 SpC added and pre-incubated at 37 °C for 1 h exhibited 91.6% and 26.7% increase in breaking force and deformation, respectively, when compared to the control.

CONCLUSIONS: Residual TGase activity in SpC played an important role in catalyzing the protein cross-linking and enhancing actomyosin gelation. SpC could be a potential ingredient for improving textural properties of fish protein gel. Copyright © 2007 Society of Chemical Industry

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