Polymerization of meat and soybean proteins by human placental calcium-activated factor XIII

Backer-Royer, Corinne De; Traore, Fatoumata; Meunier, Jean Claude

doi:10.1021/jf00023a004

Cited by 23 publications

(14 citation statements)

References 13 publications

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“…Different types of heat treatment and age of the animals from which it is extracted have different effects on the properties and gelation of collagen, which begins above 80 °C [1,11,17]. The results presented in this paper are largely consistent with previous results.…”

Section: Resultssupporting

confidence: 91%

Effects of temperature and method of heat treatment on myofibrillar proteins of pork

Vujadinović

Grujić

Tomović

et al. 2014

CI&CEQ

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Article Highlights• Thermal processing of meat cases proteins denaturation • Meat was processed by roasting and cooking in water at atmospheric pressure • By capillary electrophoresis was performed quantitative and qualitative proteins determination • Proteins during heat treatment showed a drastic decline in solubility with increasing temperature • Thermal processing by cooking had greater impact on proteins denatururation Abstract During the tests in this paper, meat processing was carried out at different temperatures in the range of 51 to 100 °C. The meat was processed by dry heat (roasting) and wet heat treatments (cooking) in water at atmospheric pressure. After heat treatment, myofibrillar proteins were extracted from solutions at constant ionic strength. Quantitative and qualitative determinations of protein fractions were performed by capillary electrophoresis. Myofibrillar proteins were also analized for fresh pork meat sample. Results obtained in fresh meat were compared with those recorded after roasting and cooking. In the fresh and thermally processed pork the following proteins were identified: myosin, light chain 3; myosin, light chain 2; troponin -C; troponin -I; myosin, light chain 1; tropomyosin; troponin -T; actin; desmin; α -actinin; C -protein; M -protein (M β ); M -protein (M α ); heavy meromyosin -HMM. For both methods of thermal processing, with increasing heat treatment temperature, concentration of soluble protein in the extract decreases rapidly after 51 °C. Cooking treatment had a more intense effect on the proteins change and denaturation than roasting.Protein denaturation in the most general form can be considered as a change in the structure of proteins, which occurs during thermal processing of meat. It is known that protein denaturation involves important changes in their structure, which may occur during thermal processing of meat. The temperature at which these changes occur is called denaturation temperature. In much of the literature, pertaining to the biochemistry of meat and studying the effect of heat treatment technology on the quality and charact-

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Section: Resultssupporting

confidence: 91%

Effects of temperature and method of heat treatment on myofibrillar proteins of pork

Vujadinović

Grujić

Tomović

et al. 2014

CI&CEQ

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“…dependence of caseinate gel was in accord with that reported in a,,-casein solution treated by guinea pig liver TGase (Nio et al, 1986). Our result on SPI was different from the results on 7s gel treated by human placental Factor XIII (Backer-Royer et al, 1992). Our microbial TGase retained enough activity and stability at pH 9 and the SPI contained other proteins besides 7s.…”

Section: Ph Dependencesupporting

confidence: 88%

Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions

Sakamoto

Kumazawa

Motoki

1994

Journal of Food Science

179

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Influence of gelling reaction conditions on the strength of several protein gels prepared with microbial transglutaminase (TGase) was investigated. A method was developed to gel proteins and measure gel breaking strength in a micro well plate. Enzyme concentration range for maximum gel breaking strength varied from 10 to 40 units/g protein. Maxima gel breaking strengths were achieved at 50°C for SPI, caseinate and gelatin and 65°C for egg yolk and egg white proteins. Optimum pH resulting in strong gels was pH 9 for SPI, caseinate, and egg yolk, and pH 6 for gelatin and egg white. Adjusting pH was promoted in egg white the formation of r-(y-glutamyl)lysine crosslinks and increased its gel breaking strength.

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“…MTG has been shown to improve texture (Mugumura et al, 1999) and gelation (De Backer-Royer et al, 1992;Lantto et al, 2005;Ahhmed et al, 2007Ahhmed et al, , 2009) of meat products. MTG catalyzes an acyl transfer reaction between a protein-or peptide-bound glutamine residue and a primary amine, which is an e-amino group of a lysine residue in a protein system.…”

Section: Introductionmentioning

confidence: 99%

Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

Sun

Arntfield

2011

Journal of Food Engineering

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Polymerization of meat and soybean proteins by human placental calcium-activated factor XIII

Cited by 23 publications

References 13 publications

Effects of temperature and method of heat treatment on myofibrillar proteins of pork

Effects of temperature and method of heat treatment on myofibrillar proteins of pork

Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions

Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking

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