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Guanghong Zhou - One of the best experts on this subject based on the ideXlab platform.
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Combination of high pressure and heat on the gelation of chicken Myofibrillar Proteins
Innovative Food Science & Emerging Technologies, 2019Co-Authors: Haibo Zheng, Minyi Han, Yun Bai, Guanghong ZhouAbstract:Abstract The effects of combinations of high pressure and heat on chicken Myofibrillar gels were investigated. High pressure was either applied simultaneously with heating (heating under pressure, HUP), before heating (PBH) or no high pressure with heat-only (HT). PBH treatment induced many similar properties in gels as did by HT treatment, except that PBH treatment promoted secondary structure transformation and formed more covalent bonds. HUP treatment resulted in less heat denaturation of the protein, induced fewer hydrophobic interactions and covalent bonds, hindered secondary and tertiary structural transformation, and formed a gel with a more porous microstructure. The gels induced by HUP treatment had softer texture and higher water holding capacity than gels induced by PBH or HT treatments. These findings suggest that high pressure with HUP treatment changes gel properties by resisting the heat-induced denaturation and gelation of Myofibrillar Proteins, while high pressure with PBH treatment alters gel properties by promoting denaturation of Myofibrillar Proteins. Industrial relevance The main constituents in meat are Myofibrillar Proteins, which are responsible for the functional properties of processed meat products. The gelation of Myofibrillar Proteins differs according to the sequence in which pressure/temperature combinations are applied. The pressure-modified protein interactions should be considered when adopting high pressure in meat product processing since the microstructure of the meat gel is affected by pressure, which would further affect water holding capacity and textural properties. HUP treatment showed its advantages in forming a fine microstructure and improving water-holding capacity.
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Effect of nitric oxide on Myofibrillar Proteins and the susceptibility to calpain-1 proteolysis.
Food chemistry, 2018Co-Authors: Rui Liu, Guanghong Zhou, Steven M. Lonergan, Edward M. Steadham, Wangang Zhang, Elisabeth J. Huff-lonerganAbstract:Abstract This study was designed to investigate the nature of modification of Myofibrillar Proteins by nitric oxide (NO) and the extent to which S-nitrosylation alters their susceptibility to calpain-1 proteolysis. Isolated myofibrils from porcine semimembranosus muscle were incubated with the NO donor S-nitrosoglutathione (GSNO) at 0, 20, 50, 250, 1000 µM for 30 min at 37 °C and then incubated with purified calpain-1. GSNO treatment decreased the thiol content of Myofibrillar Proteins and increased their intensity and amount of S-nitrosylation. GSNO caused the formation of Proteins cross-linkage through intermolecular disulfide. More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000 µM GSNO. Incubation with 250 and 1000 µM GSNO suppressed calpain-1-catalyzed cleavage of troponin-T. The data suggest that NO could change the redox state of Myofibrillar Proteins and subsequently affect the extent of proteolysis by calpain-1 in a protein-dependent manner.
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improved gel functionality of Myofibrillar Proteins incorporation with sugarcane dietary fiber
Food Research International, 2017Co-Authors: Xinbo Zhuang, Rui Liu, Wangang Zhang, Minyi Han, Yafu Liu, Lujuan Xing, Zhuangli Kang, Guanghong ZhouAbstract:Abstract The effects of sugarcane dietary fiber (SDF) on the gelation properties of porcine Myofibrillar Proteins (MP) were studied to understand its mechanism of action in improving gel functionality. Rheological tests on all composite gels (MP with SDF) showed the visco-elastic nature of MP, but the G′ significantly increased with contents of SDF and with particle size (P
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potential of high pressure homogenization to solubilize chicken breast Myofibrillar Proteins in water
Innovative Food Science and Emerging Technologies, 2016Co-Authors: Xing Che, Guanghong ZhouAbstract:Myofibrillar Proteins (MPs) of chicken breast were generally insoluble in water. The potential of high-pressure homogenization (HPH) to solubilize chicken breast MPs in water was tested. The effects of 0 psi (0.1 MPa), 10,000 psi (69 MPa), 15,000 psi (103 MPa) and 20,000 psi (138 MPa) for two passes HPH on solubility, protein profile, particle property, flow property and microstructure of MPs in water were investigated. HPH at 15,000 psi (103 MPa) could induce the suspension of MPs with small particle size species (sub-filament, oligomers or monomer structure) and high absolute zeta potential, thus enhancing the solubility, flow ability and stability without individual protein degradation. Reduction of particle size and strengthening of intermolecular electrostatic repulsion appeared to be the main reasons in solubilizing MPs in water treated with HPH. Industrial relevance The qualitative characteristics of meat products are closely related to the solubility of meat Proteins. Myofibrillar Proteins (MPs), as major part of total muscle Proteins, are generally considered to be insoluble in water. The results showed that high-pressure homogenization has potential application for solubilizing MPs in water to develop new meat-based products in the food industry.
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phosphoproteome analysis of sarcoplasmic and Myofibrillar Proteins in bovine longissimus muscle in response to postmortem electrical stimulation
Food Chemistry, 2015Co-Authors: Guanghong Zhou, Kerstin Lundström, Anders Karlsson, René LametschAbstract:Protein phosphorylation changes of the sarcoplasmic and Myofibrillar Proteins in beef longissimus muscle in response to electrical stimulation (ES) was investigated. Sarcoplasmic and Myofibrillar Proteins purified from muscle samples taken at 0, 3 and 10 h after ES were separated on SDS–PAGE and stained with phosphorous and protein specific stains. There was a significant effect of ES on phosphorylation of total sarcoplasmic and Myofibrillar Proteins (P < 0.05). However, although there an instant effect of ES on the phosphorylation level of the Myofibrillar Proteins, the ES effect on the sarcoplasmic Proteins (P < 0.05) was first observed after 3 h. Several protein bands were analyzed by LC–MS/MS, revealing that the major glycolytic Proteins, including glycogen debranching enzyme, glycogen phosphorylase and 6-phosphofructokinase probably are affected by ES together with different heat shock Proteins. This work gives an insight into the regulation of the glycolytic enzymes and muscle contraction on application of electrical stimulation.
Philippe Gatellier - One of the best experts on this subject based on the ideXlab platform.
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effect of meat cooking on physicochemical state and in vitro digestibility of Myofibrillar Proteins
Journal of Agricultural and Food Chemistry, 2008Co-Authors: Veronique Santelhoutellier, Penka Marinova, Thierry Astruc, Eleonore Greve, Philippe GatellierAbstract:The effect of meat cooking was measured on Myofibrillar Proteins from bovine M. Rectus abdominis. The heating treatment involved two temperatures (100 °C during 5, 15, 30, and 45 min and 270 °C dur...
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effect of meat cooking on physicochemical state and in vitro digestibility of Myofibrillar Proteins
Journal of Agricultural and Food Chemistry, 2008Co-Authors: Veronique Santelhoutellier, Penka Marinova, Thierry Astruc, Eleonore Greve, Philippe GatellierAbstract:The effect of meat cooking was measured on Myofibrillar Proteins from bovine M. Rectus abdominis. The heating treatment involved two temperatures (100 °C during 5, 15, 30, and 45 min and 270 °C during 1 min). Protein oxidation induced by cooking was evaluated by the level of carbonyl and free thiol groups. Structural modifications of Proteins were assessed by the measurement of their surface hydrophobicity and by their aggregation state. With the aim of evaluating the impact of heat treatment on the digestive process, Myofibrillar Proteins were then exposed to proteases of the digestive tract (pepsin, trypsin, and α-chymotrypsin) in conditions of pH and temperature that simulate stomach and duodenal digestion. Meat cooking affected Myofibrillar protein susceptibility to proteases, with increased or decreased rates, depending on the nature of the protease and the time/temperature parameters. Results showed a direct and quantitative relationship between protein carbonylation (p < 0.01) and aggregation (p < ...
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Effect of Meat Cooking on Physicochemical State and in Vitro Digestibility of Myofibrillar Proteins
Journal of Agricultural and Food Chemistry, 2008Co-Authors: Veronique Sante-lhoutellier, Penka Marinova, Thierry Astruc, Eleonore Greve, Philippe GatellierAbstract:The effect of meat cooking was measured on Myofibrillar Proteins from bovine M. Rectus abdominis. The heating treatment involved two temperatures (100 °C during 5, 15, 30, and 45 min and 270 °C during 1 min). Protein oxidation induced by cooking was evaluated by the level of carbonyl and free thiol groups. Structural modifications of Proteins were assessed by the measurement of their surface hydrophobicity and by their aggregation state. With the aim of evaluating the impact of heat treatment on the digestive process, Myofibrillar Proteins were then exposed to proteases of the digestive tract (pepsin, trypsin, and R-chymotrypsin) in conditions of pH and temperature that simulate stomach and duodenal digestion. Meat cooking affected Myofibrillar protein susceptibility to proteases, with increased or decreased rates, depending on the nature of the protease and the time/temperature parameters. Results showed a direct and quantitative relationship between protein carbonylation (p < 0.01) and aggregation (p < 0.05) induced by cooking and proteolytic susceptibility to pepsin. However, no such correlations have been observed with trypsin and R-chymotrypsin.
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effect of oxidation on in vitro digestibility of skeletal muscle Myofibrillar Proteins
Journal of Agricultural and Food Chemistry, 2007Co-Authors: Veronique Santelhoutellier, Laurent Aubry, Philippe GatellierAbstract:The objective of this study was to investigate the effect of chemical oxidation on Myofibrillar protein digestibility. Myofibrils were prepared from pig M. longissimus dorsi and oxidized by a hydroxyl radical generating system. Oxidative modifications of Proteins were assessed by the carbonyl content, surface hydrophobicity, electrophoresis, and immunoblotting. Oxidized or nonoxidized Myofibrillar Proteins were then exposed to proteases of the digestive tract (pepsin, trypsin, and α-chymotrypsin). Results showed a direct and quantitative relationship between protein damages by hydroxyl radical and loss of protein digestibility. Keywords: Myofibrils; carbonyl; hydrophobicity; electrophoresis; immunoblotting; proteolysis; digestibility
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chemical oxidation decreases proteolytic susceptibility of skeletal muscle Myofibrillar Proteins
Meat Science, 2006Co-Authors: Martine Morzel, Philippe Gatellier, Thierry Sayd, M Renerre, Elisabeth LavilleAbstract:The objective of this study was to investigate the effect of chemical oxidation on proteolysis susceptibility of Myofibrillar Proteins. Myofibrils were prepared from pig M. longissimus dorsi and oxidised by a hydroxyl radical generating system. Protein oxidation level was measured by the carbonyl content, free thiol group content and bityrosine formation. Oxidised or non-oxidised Myofibrillar Proteins were exposed to papain and proteolysis was estimated by fluorescence using fluorescamine. Oxidation of Myofibrillar Proteins was dependent upon the oxidising agent concentration. Disulfide bridge and bityrosine formation indicated that oxidation by OH° can induce protein polymerization. Electrophoretic study showed that myosin was the protein most sensitive to oxidation. Results showed a direct and quantitative relationship between protein damages by hydroxyl radical and decreased proteolytic susceptibility. Electrophoretic observations suggest that polymerization and aggregation may explain in part decreased susceptibility of Myofibrillar Proteins to proteolysis.
Tao Yin - One of the best experts on this subject based on the ideXlab platform.
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Effects of vacuum chopping on physicochemical and gelation properties of Myofibrillar Proteins from silver carp (Hypophthalmichthys molitrix).
Food chemistry, 2017Co-Authors: Shanbai Xiong, Juan You, Qilin Huang, Tao YinAbstract:Abstract Physicochemical and gelation properties of Myofibrillar Proteins from silver carp surimi as affected by chopping under different vacuum degrees (0, 0.01, 0.02, 0.04, 0.06 and 0.08 MPa) were investigated. With the increase of vacuum degree, size and quantity of air bubbles in surimi paste decreased, disulfide bond content of Myofibrillar Proteins decreased significantly (p .05), while surface hydrophobicity of Myofibrillar Proteins increased gradually (p
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effects of ozone treatments on the physicochemical changes of Myofibrillar Proteins from silver carp hypophthalmichthys molitrix during frozen storage
Journal of Food Quality, 2017Co-Authors: Rongrong Zhang, Shanbai Xiong, Juan You, Ru Liu, Tao YinAbstract:Physicochemical changes of Myofibrillar Proteins from silver carp surimi during frozen storage as affected by two manners of ozone treatments were investigated. For preparation of surimi treated with ozone, ozone water (8 mg/L) was used in either the first (To1) or the second (To2) cycle of rinsing. As compared with control samples (Tc) (rinsing two cycles with water), Myofibrillar Proteins from To1 surimi showed slightly lower free sulfhydryl contents and higher surface hydrophobicity throughout frozen storage and lower Ca2+-ATPase activities after 30 d. To2 did not significantly ( ) affect these physicochemical properties, indicating that Myofibrillar Proteins structure was well maintained. Consequently, To1 significantly ( ) decreased breaking force of surimi gels while To2 did not significantly ( ) affect gel breaking force. In addition, the whiteness of surimi gels was increased more obviously by To2 than by To1. The results indicate that To2 could be used as a mild oxidation treatment for improving white color of silver carp surimi without negatively affecting gel texture.
Minyi Han - One of the best experts on this subject based on the ideXlab platform.
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Combination of high pressure and heat on the gelation of chicken Myofibrillar Proteins
Innovative Food Science & Emerging Technologies, 2019Co-Authors: Haibo Zheng, Minyi Han, Yun Bai, Guanghong ZhouAbstract:Abstract The effects of combinations of high pressure and heat on chicken Myofibrillar gels were investigated. High pressure was either applied simultaneously with heating (heating under pressure, HUP), before heating (PBH) or no high pressure with heat-only (HT). PBH treatment induced many similar properties in gels as did by HT treatment, except that PBH treatment promoted secondary structure transformation and formed more covalent bonds. HUP treatment resulted in less heat denaturation of the protein, induced fewer hydrophobic interactions and covalent bonds, hindered secondary and tertiary structural transformation, and formed a gel with a more porous microstructure. The gels induced by HUP treatment had softer texture and higher water holding capacity than gels induced by PBH or HT treatments. These findings suggest that high pressure with HUP treatment changes gel properties by resisting the heat-induced denaturation and gelation of Myofibrillar Proteins, while high pressure with PBH treatment alters gel properties by promoting denaturation of Myofibrillar Proteins. Industrial relevance The main constituents in meat are Myofibrillar Proteins, which are responsible for the functional properties of processed meat products. The gelation of Myofibrillar Proteins differs according to the sequence in which pressure/temperature combinations are applied. The pressure-modified protein interactions should be considered when adopting high pressure in meat product processing since the microstructure of the meat gel is affected by pressure, which would further affect water holding capacity and textural properties. HUP treatment showed its advantages in forming a fine microstructure and improving water-holding capacity.
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improved gel functionality of Myofibrillar Proteins incorporation with sugarcane dietary fiber
Food Research International, 2017Co-Authors: Xinbo Zhuang, Rui Liu, Wangang Zhang, Minyi Han, Yafu Liu, Lujuan Xing, Zhuangli Kang, Guanghong ZhouAbstract:Abstract The effects of sugarcane dietary fiber (SDF) on the gelation properties of porcine Myofibrillar Proteins (MP) were studied to understand its mechanism of action in improving gel functionality. Rheological tests on all composite gels (MP with SDF) showed the visco-elastic nature of MP, but the G′ significantly increased with contents of SDF and with particle size (P
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low field nmr study of heat induced gelation of pork Myofibrillar Proteins and its relationship with microstructural characteristics
Food Research International, 2014Co-Authors: Peng Wang, Minyi Han, Guanghong ZhouAbstract:Abstract The changes of water mobility and fractal dimension (Df) during pork Myofibrillar Proteins (PMP) heat-induced gelation were investigated using low-field nuclear magnetic resonance (NMR) and image analysis, respectively. The NMR data were related to the gel microstructure which was explained as fractal dimension and pore size using principal component analysis (PCA). Distributed exponential analysis of the T2 relaxation revealed that three water components corresponding to the three water molecule states exist during the heat-induced gelation. A significant change of T2 was occurred when the temperature increased, T21 relaxation times decreased significantly from 403.70 ms to 231.01 ms with the temperature increasing from 50 to 70 °C. The fraction of T21 distributions declined from 99.27% to 77.01% as the temperature increased from 40 to 60 °C. Pronounced different gel network structure was observed during the Myofibrillar Proteins heat-induced gelation and different Df which was determined by box count method was found between all treatments although evidencing a narrow scale range (from 2.835 to 2.860). Good correlations were detected between the NMR T2 parameters and microstructural data. Overall, combined low-field NMR, image analysis and PCA provide powerful tools for elucidating the pork Myofibrillar protein heat-induced gelation.
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raman spectroscopic study of the effects of microbial transglutaminase on heat induced gelation of pork Myofibrillar Proteins and its relationship with textural characteristics
Food Research International, 2011Co-Authors: Hongye Chen, Minyi HanAbstract:Abstract The effects of microbial transglutaminase (MTG) on heat-induced gelation of pork Myofibrillar Proteins (PMP) structural changes, textural properties were studied by Raman spectroscopy and texture profile analysis (TPA), respectively. And the relationships between the structural changes and textural characteristics were estimated by principal component analysis (PCA). Changes in the Raman spectra were interpreted as the occurrence of secondary structural changes in Myofibrillar Proteins with MTG added. Modifications in the amide I (1600–1700 cm − 1 ) regions indicated a significant (p − 1 and fraction of α-helix. The samples are closely grouped in a cluster defined by level of MTG.
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Raman spectroscopic study of heat-induced gelation of pork Myofibrillar Proteins and its relationship with textural characteristic
Meat science, 2010Co-Authors: Minyi Han, Ying Fei, Guanghong ZhouAbstract:Structural changes, textural properties and their relationships in pork Myofibrillar Proteins (PMP) were studied by Raman spectroscopy, texture profile analysis (TPA) and principal component analysis (PCA). Raman spectroscopy analysis revealed the occurrence of secondary structural changes in Myofibrillar Proteins. Modifications in the amide I (1600-1700 cm(-1)) and amide III (1200-1300 cm(-1)) regions indicated a significant (p
Akihito Hattori - One of the best experts on this subject based on the ideXlab platform.
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Physicochemical properties of water‐soluble Myofibrillar Proteins prepared from chicken breast muscle
Animal Science Journal, 2004Co-Authors: Yukiko Ito, Ryuichi Tatsumi, Jun-ichi Wakamatsu, Takanori Nishimura, Shinji Toki, Takashi Omori, Hiroshi Ide, Akihito HattoriAbstract:The solubility of skeletal muscle Myofibrillar Proteins in water was examined. The solubility of the Proteins was found to be sensitive to ionic strength and pH of the solution. At the ionic strength of less than 12 mM and neutral pH, more than 80% of Myofibrillar Proteins were solubilized. Heating at a temperature of more than 70°C was required for the Proteins to retain their solubility. The solubility of freeze-dried protein powder prepared from water-soluble Myofibrillar Proteins was also examined, and it was found that addition of trehalose and heating were essential for re-solubilization in water. Amino acid composition of water-soluble Myofibrillar Proteins was found to be almost the same as that of Myofibrillar Proteins.
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The solubilization of Myofibrillar Proteins of vertebrate skeletal muscle in water
Animal Science Journal, 2003Co-Authors: Yukiko Ito, Ryuichi Tatsumi, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito HattoriAbstract:Myofibrillar Proteins of vertebrate skeletal muscles are insoluble in solutions of ionic strength that approximate physiological conditions. We established a method to solubilize more than 80% of chicken breast muscle Myofibrillar Proteins in water for the use of meat as a source of food protein. SDS-polyacrylamide gel electrophoretic patterns of water-soluble Myofibrillar Proteins demonstrated that all identified Myofibrillar Proteins except connectin/titin were soluble in water. A part of α-actinin was released from myofibrils by repeated washing with 2.5 mmol/L NaCl and 5 mmol/L L-histidine solution, and subsequent destruction of connectin/titin in washed myofibrils by ultrasonication resulted in solubilization of a large fraction of chicken breast muscle Myofibrillar Proteins in water. Myofibrillar Proteins of chicken leg, pork loin, beef shoulder loin, and lamb were also solubilized in water using this procedure.
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detection of giant Myofibrillar Proteins connectin and nebulin by electrophoresis in 2 polyacrylamide slab gels strengthened with agarose
Analytical Biochemistry, 1995Co-Authors: Ryuichi Tatsumi, Akihito HattoriAbstract:Abstract We have established an improved method of sodium dodecyl sulfate-polyacrylamide gel electrophoresis to facilitate analysis of giant Myofibrillar Proteins connectin and nebulin, whose molecular masses are about 3000 and 700 kDa, respectively. This method consists of 2% polyacrylamide slab gels strengthened with agarose and a specific buffer system. Our 2% polyacrylamide slab gels are superior to usual 1.8 or 2% polyacrylamide disc gels in preparation, handling, and resolution.
