Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing∗

Xiong, Youling L.

doi:10.1080/10408399409527665

Cited by 165 publications

(119 citation statements)

References 124 publications

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“…The high solubility of protein is thought to only alter the quantity of the effective gelling components, rather than affecting the specific protein bonds in the gel matrix. This hypothesis is supported by the observation that the proteins form substantially weaker gels as the pH is raised from 6.0 to 7.0 (Xiong, 1994). Thus, we propose that the different gel strength of MP-FG induced by pH is ascribed to the protein-protein and protein-FG interactions that form the gel structures with various texture properties.…”

Section: Effects Of Ph On the Gel Strength Of Thermal Mp-fg Gelsupporting

confidence: 67%

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

Pan

Feng

Sun

et al. 2016

CyTA - Journal of Food

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Flaxseed gum (FG) was reported to enhance the water holding capacity and thermal stability of myofibrillar protein (MP). However, the role of pH in the interaction of MP and FG is still unclear. The aim of this study was to evaluate gelling properties and physicochemical properties of MP-FG gel at various pH values, to explore the mechanism. The results reveal that higher pH value could increase the water holding capacity of MP-FG gels and the highest gel strength is achieved at pH 6.5. Raman spectroscopic analysis reveals that decreasing the pH from 7.5 to 5.5 induces the partial transformation of α-helices into β-sheets. At the same pH value, addition of FG also leads to the transformation of α-helices into β-sheets, affecting the formation of gel. The storage modulus (G') values and gelation rates during gelation process gradually declines with the increasing pH, which might be conducted to form a fine dense network.Las propiedades térmicas de gelificación y el mecanismo de la proteína miofibrilar porcina que contiene goma de linaza con diferentes valores pH RESUMEN Se declaró que la goma de linaza (FG) mejora la capacidad de retención del agua y la estabilidad térmica de la proteína miofibrilar (MP). Sin embargo, el papel del pH en la interacción de MP y FG aún no está claro. El objetivo de este estudio fue evaluar las propiedades de gelificación y las propiedades fisicoquímicas del gel MP-FG con diferentes valores pH para explorar su mecanismo. Los resultados revelan que un valor pH mayor podría aumentar la capacidad de retención de agua de los geles MP-FG, además la mayor fuerza del gel se consiguió con un pH 6,5. El análisis espectroscópico Raman reveló que reducir el pH de 7,5 a 5,5 induce a la transformación parcial de hélices α a láminas beta β. Con el mismo valor pH, la adición de FG también conlleva a la transformación de hélices α a láminas beta β, afectando la formación de gel. Los valores del módulo de almacenamiento (G') y el índice de gelificación durante el proceso de gelificación se reducen gradualmente con el incremento del pH, lo cual puede conducir a la formación de una densa red. ARTICLE HISTORY

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Section: Effects Of Ph On the Gel Strength Of Thermal Mp-fg Gelsupporting

confidence: 67%

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

Pan

Feng

Sun

et al. 2016

CyTA - Journal of Food

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“…Charged alginate polymers in meat system compete for water to form a viscous sol or visco-elastic gel, thereby interfering with their structure-forming ability and gel matrix formation (Tolstoguzov, 1991;Xiong and Blanchard, 1993). In structured beef, Xiong (1994) reported that addition of connective tissue reduced the stability of beef batters. Sci., 5 (1): 14-48, 2015Hughes et al (1997 found increased emulsion stability in frankfurters formulated with carrageenan and 0.7% carrageenan incorporation resulted in the highest (p<0.05) emulsion stability (as total volume released) compared to 0.5% and controls.…”

Section: Quality Of Restrucutred Meat Products Cooking Yieldmentioning

confidence: 99%

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Reddy¹,

Mandal²,

Sen³

et al. 2014

International J. of Meat Science

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To provide the consumer with a highly palatable product at a reasonable cost is the main objective of any food industry. Particular to meat industry, utilization of less valuable carcasses and carcass cuts and carcass components (plates, flanks, shanks, etc.) is of prime interest in periods of economic pressure. One such relevantly new technological approach is restructuring technology, which enables the production of value-added meat products from low value cuts and trimmings of carcasses. Although the economics and processing of restructuring meats appear favourable to producing a product that has the palatability attributes that are between an intact muscle steak and ground meat. This review of restructured meat products discuss the actual science and technology behind the restructuring of muscles, how muscle chunks are binding each together at protein molecules stage, factors influencing the meat pieces binding, type of restructuring methodologies, quality attributes of restructured meat products, problems of oxidation, use of natural antioxidants and recommends research needs for the future.

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“…It is widely accepted that the myofibrillar proteins are the main responsible for the technological quality of the meat products (Xiong, 1994). Previous works have informed on the physico-chemical, biochemical, and functional properties of major myofibrillar proteins from squid Illexargentinus (Paredi, Roldán, & Crupkin, 2006;Mignino & Paredi, 2006).…”

Section: Introductionmentioning

confidence: 99%

Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

Mignino¹,

Crupkin²,

Paredi³

2013

JFR

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Actomyosin (AM) of mantle and fin from squid was stored at 2-4°C and the possible presence of proteolytic activity was investigated. Similar SDS-PAGE 10% patterns were obtained with both AM at zero time of storage. In absence of protease inhibitors, a decrease in the intensity of the band of the myosin heavy chain (MHC) and an increase in those of 155 kDa and 55 kDa bands of stored AM was observed. In presence of either PMSF (phenylmethylsulfonyl fluoride) or EDTA (ethylenediaminetetraacetic acid) both AM showed a minor degradation of the MHC, being the EDTA more effective. Proteolytic changes were accompanied by a significant increase (p < 0.05) in the proteinsurface hydrophobicity, (So: 1-anilino-8-naphtalene sulfonic acid (ANS)), the emulsion activity index (EAI) and the emulsion stability (ES) at 24 h of storage. At the same time, the reduced viscosity (VER) decreased significantly (p < 0.05). No significative changes (p > 0.05) in VER, IAE and ES of both AM occur in presence of protease inhibitors.A proteolytic activity closely associate with actomyosin from squid mantle and fin, was detected. Both serine and metalloproteinase activities were responsible for the autolysis of stored actomyosin. The best emulsifiying properties were obtained with AM without inhibitors. Because of this fins proteins could be and inexpensive source of functional ingredients with potential application as emulsifier agents in food product.

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Myofibrillar protein from different muscle fiber types: Implications of biochemical and functional properties in meat processing∗

Cited by 165 publications

References 124 publications

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

Thermal gelling properties and mechanism of porcine myofibrillar protein containing flaxseed gum at various pH values

Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review

Proteolytic Activity in Actomyosinfrom Mantle and Fin of Squid (Illexargentinus) Stored at 2-4°C. Influence on the Physicochemical and Functional Properties of the Protein

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