Effects of high pressure modification on conformation and gelation properties of myofibrillar protein.

The effects of high pressure (HP) treatment (100-500MPa) on conformation and gelation properties of myofibrillar protein (MP) were investigated. As pressure increased (0.1-500MPa), α-helix and β-sheet changed into random coil and β-turn, proteins unfolded to expose interior hydrophobic and sulfhydryl groups, therefore surface hydrophobicity and formation of disulfide bonds were strengthened. At 200MPa, protein solubility and gel hardness reached their maximum value, particle size had minimum value, and gel microstructure was dense and uniform. DSC data showed that actin and myosin completely denatured at 300MPa and 400MPa, respectively. Rheological modulus (G' and G″) of HP-treated MP decreased as pressure increased during thermal gelation. Moderate HP treatment (≦200MPa) strengthened gelation properties of MP, while stronger HP treatment (⩾300MPa) weakened the gelation properties. 200MPa was the optimum pressure level for modifying MP conformation to improve its gelation properties.

[1]  K. Chawla,et al.  Mechanical Behavior of Materials , 1998 .

[2]  J. J. Macfarlane,et al.  Modification of the heat-setting characteristics of myosin by pressure treatment. , 1984, Meat science.

[3]  A. Mauri,et al.  Physicochemical and structural properties of amaranth protein isolates treated with high pressure , 2012 .

[4]  B. Farkas,et al.  High pressure effects on heat-induced gelation of threadfin bream (Nemipterus spp.) surimi , 2015 .

[5]  S. Kasapis,et al.  Structural modification in condensed soy glycinin systems following application of high pressure , 2016 .

[6]  G. Ferrari,et al.  Effects of high hydrostatic pressure on the conformational structure and the functional properties of bovine serum albumin , 2016 .

[7]  Yinji Chen,et al.  Chemical forces study of heat-induced myofibrillar protein gel as affected by partial substitution of NaCl with KCl, MgCl2 and CaCl2 , 2016 .

[8]  Stéphanie Jung,et al.  Effect of high pressure treatment on ovotransferrin. , 2012, Food chemistry.

[9]  A. Mullen,et al.  High pressure induced changes in beef muscle proteome: correlation with quality parameters. , 2014, Meat science.

[10]  Chia-Ling Jao,et al.  Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Orechromis niloticus) on hydrostatic pressure treatment , 2007 .

[11]  Y. Xiong,et al.  Oxidative modification of amino acids in porcine myofibrillar protein isolates exposed to three oxidizing systems , 2007 .

[12]  S. Vaudagna,et al.  High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins , 2014 .

[13]  E. Hückel,et al.  The nature of the chemical bond and the structure of molecules and crystals. — An Introduction to modern structural chemistry. von Linus Pauling. 429 S.mit 72 Fig. Ithaka, New‐York. Cornell University Press. Preis geb. 4,50 Dollar , 1940, Zeitschrift für Elektrochemie und angewandte physikalische Chemie.

[14]  Li-te Li,et al.  Influence of high pressure on conformational changes of soybean glycinin , 2003 .

[15]  H. Martens,et al.  Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry , 1980 .

[16]  M. Ngadi,et al.  Effect of high pressure on rheological characteristics of liquid egg , 2003 .

[17]  I. V. D. Plancken,et al.  Combined effect of high pressure and temperature on selected properties of egg white proteins , 2005 .

[18]  M. de Lamballerie-Anton,et al.  Physicochemical modifications of high-pressure-treated soybean protein isolates. , 2004, Journal of agricultural and food chemistry.

[19]  Guang-hong Zhou,et al.  The mechanism of high pressure-induced gels of rabbit myosin , 2012 .

[20]  H. Ramaswamy,et al.  High pressure gelation of soy proteins : Effect of concentration, pH and additives , 2008 .

[21]  A. Borderías,et al.  Effect of high pressure on reduced sodium chloride surimi gels , 2015 .

[22]  J. Ahmed,et al.  Novel Food Processing : Effects on Rheological and Functional Properties , 2016 .

[23]  Monika Sharma,et al.  Effect of High Pressure Treatment on Rheological Characteristics of Egg Components , 2015 .

[24]  R. López-Fandiño,et al.  Skim milk protein distribution as a result of very high hydrostatic pressure , 2015 .

[25]  E Morild,et al.  The theory of pressure effects on enzymes. , 1981, Advances in protein chemistry.

[26]  F. Ma,et al.  Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan. , 2013, Meat science.

[27]  Li Liu,et al.  Effects of high pressure on the physicochemical and functional properties of peanut protein isolates , 2014 .

[28]  P. Linko,et al.  Mechanism of High Pressure Denaturation of Proteins , 1996 .

[29]  Hosahalli S. Ramaswamy,et al.  Effect of high-pressure treatment on rheological, thermal and structural changes in Basmati rice flour slurry , 2007 .

[30]  Linus Pauling,et al.  The Nature of the Chemical Bond and the Structure of Molecules and Crystals , 1941, Nature.

[31]  J. Culioli,et al.  Effects of high pressure on meat: A review. , 1997, Meat science.

[32]  J. Culioli,et al.  Thermal Gelation of Brown Trout Myofibrils: Effect of Muscle Type, Heating Rate and Protein Concentration , 2008 .

[33]  H. Ramaswamy,et al.  Back Extrusion Rheology for Evaluating the Transitional Effects of High Pressure Processing of Egg Components , 2015 .

[34]  Paul R. Carey,et al.  Biochemical Applications of Raman and Resonance Raman Spectroscopies , 1982 .

[35]  Yinji Chen,et al.  Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. , 2015, Food chemistry.

[36]  Alain J. P. Alix,et al.  Fast determination of the quantitative secondary structure of proteins by using some parameters of the Raman Amide I band , 1988 .