Abstract

The objective of this study was to observe the interactions between salt-soluble proteins from beef and seaweed (Eucheuma cottonii) flour and its effect to the quality of the produced protein gel. The study was conducted as experimental research with two factorials completely randomized design. The effect of different NaCl (2.0%; 2.5%; 3.0%; and 3.5%) and Eucheuma cottonii flour (5%; 10%; and 15%) concentrations was observed to the physical and proximate quality of the protein gel matrix. The observed gel quality variables include pH, gel strength, color (L, a*, and b*), moisture, protein, and fat content. The gel was gelatinized at 90°C for 20 min and cooled down at 4°C for 12 h. The results showed that there was no interaction effect found on all of observed variables. However, a highly significant effect (P<0.01) was found on the ash content with different salt concentrations, while different Eucheuma cottonii flour concentrations improved the gel strength (P<0.01) and significantly gave darker (P<0.01) color. The effect of Eucheuma cottonii flour on the physicochemical properties of the gel was concentration dependent. Therefore, this study concludes that Eucheuma cottonii flour showed a potential as binding or filling agent to form strong gel matrix in processed meat products.

Highlights

  • Beef contains around 16 to 22% protein consisting of 11.5% myofibril, 5.5% sarcoplasmic, and 3% stromal protein (Soeparno, 2009)

  • The salt myofibril proteins extraction is known to be affected by salt concentration, with the common extraction was done with salt solution at 0.3 M or higher

  • Materials The materials used in this study are salt-soluble protein gel fraction and Eucheuma cottonii flour

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Summary

Introduction

Beef contains around 16 to 22% protein consisting of 11.5% myofibril, 5.5% sarcoplasmic, and 3% stromal protein (Soeparno, 2009). The myosin and actin extraction of beef is affected by several factors, such as salt concentration, pH, and non-protein polymers (Sun et al, 2011; Sun dan Holley, 2011). The salt myofibril proteins extraction is known to be affected by salt concentration, with the common extraction was done with salt solution at 0.3 M or higher. The addition of salt during meatbased food production would extract the salt soluble protein from meat (myosin and actin), and increase the meat binding capacity, yield, and juiciness (Purnomo, 2012). Research by Keever (2011) that used varied salt concentrations (0.5% to 3.5%) showed that the highest extracted protein was found on 3.5% salt addition

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