The characteristics of selected physico-chemical properties of chemically modified myofibrillar protein

Abstract

The objective of the present research was to investigate the influence of chemical modification and method of preservation of separated myofibrillar proteins on their physico-chemical properties. Myofibrillar proteins were the subject to succinylation or acylation and after modification one part of each preparation was lyophilised, the second part was spray dried and the third part was frozen. The chemical composition of protein preparations did not change significantly after any method of treatment. The process of chemical modification influenced the waterholding capacity and protein digestibility in vitro. Modified samples absorbed less water than standards and also were less susceptible to enzymatic hydrolysis. The shape of sorption isotherms of modified proteins was typical for hygroscopic products and hysteresis loops were observed.

Chemical and Enzymatic Protein Modifications and Functionality Enhancement

“…Succinylation improves solubility Ma 1984;Ponnampalam et al 1988;Sitohy, Sharobeem, and Abdel-Ghany 1992;Bae and Jang 1999), emulsifying property (Franzen and Kinsella 1976;Thompson and Reyes 1980;Ma 1984;Ponnampalam et al 1988;Gueguen et al 1990;Sitohy, Sharobeem, and Abdel-Ghany 1992;Bae and Jang 1999;Lawal and Adebowale 2006), foaming capacity (Franzen and Kinsella 1976;Gueguen et al 1990;Sitohy, Sharobeem, and Abdel-Ghany 1992;Krause 2002;Lawal and Adebowale 2006), and gelling property (Ma and Holme 1982;Bae and Jang 1999). Both succinylation and acetylation decrease digestibility (Eisele, Brekke, and McCurdy 1981;Pomianowski, Borowski, and Danowska-Oziewicz 1999), protein efficiency ratio (Groninger and Miller 1979;Goulet et al 1987), and bioavailability (King, Ball, and Garlich 1981), and have no specific biological activity in vivo.…”

“…The imidazole group of histidine residue and the thiol group of cysteine residue are rarely acylated because the reaction products are hydrolyzed in an aqueous solution. The alcoholic hydroxyl group of serine Franzen and Kinsella (1976); Barman, Hansen, and Mossey (1977); Brinegar and Kinsella (1980) Fish protein Groninger and Miller (1979) Myofibrillar protein ; Eisele, Brekke, and McCurdy (1981); Pomianowski, Borowski, and Danowska-Oziewicz (1999) Oat protein Ma (1984); Goulet et al (1987); Ponnampalam et al (1988) Faba bean protein Krause and Schwenke (1996) Jack bean protein Lawal and Adebowale (2006) Pea protein Szymkiewicz and Jedrychowski (2008) Rapeseed protein Schwenke, Dahme, and Wolter (1998); Gueguen et al (1990) Peanut protein Beuchat (1977) Flax protein Shahidi and Wanasundara (1998) Wheat protein Grant (1973); Sitohy, Sharobeem, and AbdelGhany (1992) Corn protein Sitohy, Sharobeem, and Abdel-Ghany (1992) Rice bran protein Bae and Jang (1999) Whey protein Thompson and Reyes (1980) Egg protein Ma and Holme (1982); Sitohy, Sharobeem, and Abdel-Ghany (1992) Milk protein Puigserver et al (1979aPuigserver et al ( , 1979b Yeast protein Kinsella and Shetty (1979) Downloaded by [University of Otago] at 23:12 26 November 2016 and threonine residues is not easily acylated in an aqueous solution because it is a weak nucleophile.…”