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1.
Crit Rev Food Sci Nutr ; 57(15): 3260-3280, 2017 Oct 13.
Article in English | MEDLINE | ID: mdl-26647280

ABSTRACT

The qualitative characteristics of meat products are closely related to the functionality of muscle proteins. Myofibrillar proteins (MPs), comprising approximately 50% of total muscle proteins, are generally considered to be insoluble in solutions of low ionic strength (< 0.2 M), requiring high concentrations of salt (> 0.3 M) for solubilization. These soluble proteins are the ones which determine many functional properties of meat products, including emulsification and thermal gelation. In order to increase the utilization of meat and meat products, many studies have investigated the solubilization of MPs in water or low ionic strength media and determining their functionality. However, there still remains a lack of systematic information on the functional properties of MPs solubilized in this manner. Hence, this review will explore some typical techniques that have been used. The main procedures used for their solubilization, the fundamental principles and their functionalities in water (low ionic strength medium) are comprehensively discussed. In addition, advantages and disadvantages of each technique are summarized. Finally, future considerations are presented to facilitate progress in this new area and to enable water soluble muscle MPs to be utilized as novel meat ingredients in the food industry.


Subject(s)
Muscle Proteins/chemistry , Osmolar Concentration , Meat , Solubility , Water/chemistry
2.
Meat Sci ; 115: 34-40, 2016 May.
Article in English | MEDLINE | ID: mdl-26802614

ABSTRACT

Eight pale, soft and exudative (PSE) and eight reddish-pink, firm and non-exudative (RFN) porcine longissimus muscle samples were selected based on pH and L* at 1h postmortem (PM), and drip loss at 24h PM, and used to evaluate the cellular calcium and apoptosis status. We found that SERCA1 was decreased, while IP3R was decreased in PSE meat (P<0.05), indicative of the overloaded sarcoplasmic calcium status. In PSE meat, the pro-apoptotic factor BAX was increased while the anti-apoptotic factor Bcl-2 was decreased (P<0.05). The significantly increased activity of caspase 3 and the expression of its cleavage fragment suggested higher apoptotic potential in PSE meat compared with RFN meat (P<0.05). Moreover, the significantly higher expression level of cytochrome C (P<0.05) suggests the important role of mitochondria during apoptosis appearance in PSE meat. Taken together, our data inferred that the calcium channel disorder present in PSE meat was associated with the increased apoptotic potential.


Subject(s)
Calcium Channels/metabolism , Endoplasmic Reticulum Stress , Red Meat/analysis , bcl-2-Associated X Protein/metabolism , Animals , Calcium/metabolism , Calcium Channels/genetics , Caspase 3/genetics , Caspase 3/metabolism , Color , Cytochromes c/genetics , Cytochromes c/metabolism , Endoplasmic Reticulum/metabolism , Food Handling , Food Quality , Hydrogen-Ion Concentration , Muscle Proteins/genetics , Muscle Proteins/metabolism , Muscle, Skeletal/chemistry , Sarcoplasmic Reticulum Calcium-Transporting ATPases/genetics , Sarcoplasmic Reticulum Calcium-Transporting ATPases/metabolism , Swine , bcl-2-Associated X Protein/genetics
3.
Meat Sci ; 97(2): 244-8, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24598071

ABSTRACT

Our aim was to achieve a single-step pressure-heat process that would produce tender, juicy beef steaks from meat that would otherwise be tough when cooked. Steak portions (25mm thick) from hind-quarter muscles were subjected to heat treatment at 60, 64, 68, 72 or 76°C for 20min, with or without simultaneous application of high pressure (200MPa). Control steaks were heated at 60°C for 20min with or without pressure and cooked at 80°C for 30min. Compared with heat alone, pressure treatment resulted in higher lightness scores at all temperatures and overall yield was improved by pressure treatment at each temperature. Even at 76°C, the overall water losses were <10% compared with >30% for heat alone. Meat tenderness (peak shear force) was improved for the pressure-heat samples at temperatures above 64°C, and was optimal at 76°C. Therefore, subject to microbial evaluation, this single-step pressure-heat process could be used to produce tender, high moisture content steaks ready for consumption.


Subject(s)
Color , Food Handling/methods , Hydrostatic Pressure , Meat/analysis , Stress, Mechanical , Temperature , Water , Animals , Cattle , Muscle, Skeletal
4.
Crit Rev Food Sci Nutr ; 53(7): 770-86, 2013.
Article in English | MEDLINE | ID: mdl-23638936

ABSTRACT

The application of high pressure offers some interesting opportunities in the processing of muscle-based food products. It is well known that high-pressure processing can prolong the shelf life of meat products in addition to chilling but the pressure-labile nature of protein systems limits the commercial range of applications. High pressure can affect the texture and gel-forming properties of myofibrillar proteins and, hence, has been suggested as a physical and additive-free alternative to tenderize and soften or restructure meat and fish products. However, the rate and magnitude at which pressure and temperature effects take place in muscles are variable and depend on a number of circumstances and conditions that are still not precisely known. This review provides an overview of the current knowledge of the effects of high pressure on muscle tissue over a range of temperatures as it relates to meat texture, microstructure, color, enzymes, lipid oxidation, and pressure-induced gelation of myofibrillar proteins.


Subject(s)
Chemical Phenomena , Meat Products/analysis , Pressure , Animals , Calpain/analysis , Calpain/chemistry , Cathepsins/analysis , Cathepsins/chemistry , Cattle , Chickens , Color , Fishes , Food Handling , Lipid Metabolism , Muscle Proteins/analysis , Muscle Proteins/chemistry , Muscle, Skeletal/chemistry , Temperature
5.
J Exp Biol ; 215(Pt 2): 343-50, 2012 Jan 15.
Article in English | MEDLINE | ID: mdl-22189778

ABSTRACT

Exposure of prawns to dark- or light-coloured substrates is known to trigger a strong colour adaptation response through expansion or contraction of the colouration structures in the prawn hypodermis. Despite the difference in colour triggered by this adaptive response, total levels of the predominant carotenoid pigment, astaxanthin, are not modified, suggesting that another mechanism is regulating this phenomenon. Astaxanthin binds to a specific protein called crustacyanin (CRCN), and it is the interaction between the quantities of each of these compounds that produces the diverse range of colours seen in crustacean shells. In this study, we investigated the protein changes and genetic regulatory processes that occur in prawn hypodermal tissues during adaptation to black or white substrates. The amount of free astaxanthin was higher in animals adapted to dark substrate compared with those adapted to light substrate, and this difference was matched by a strong elevation of CRCN protein. However, there was no difference in the expression of CRCN genes either across the moult cycle or in response to background substrate colour. These results indicate that exposure to a dark-coloured substrate causes an accumulation of CRCN protein, bound with free astaxanthin, in the prawn hypodermis without modification of CRCN gene expression. On light-coloured substrates, levels of CRCN protein in the hypodermis are reduced, but the carotenoid is retained, undispersed in the hypodermal tissue, in an esterified form. Therefore, the abundance of CRCN protein affects the distribution of pigment in prawn hypodermal tissues, and is a crucial regulator of the colour adaptation response in prawns.


Subject(s)
Carrier Proteins/metabolism , Color , Penaeidae/physiology , Pigmentation , Acclimatization , Adaptation, Physiological , Animals , Arthropod Proteins/metabolism , Carrier Proteins/genetics , Chromatography, High Pressure Liquid , Diet , Environment , Epithelium/metabolism , Gene Expression Regulation , Hot Temperature , Molting , Organ Specificity , Penaeidae/genetics , Penaeidae/growth & development , Real-Time Polymerase Chain Reaction , Xanthophylls/metabolism
6.
Meat Sci ; 84(3): 390-9, 2010 Mar.
Article in English | MEDLINE | ID: mdl-20374801

ABSTRACT

Tenderness of beef M. Sternomandibularis was tough when cooked from both raw, and when previously heated (60 degrees C, 20 min), whereas a significant improvement in tenderness was achieved when pressure-heat (P-H) treated muscle (200 MPa, 60 degrees C, 20 min) was cooked. In order to determine the mechanism for this improvement, connective tissue, myofibrillar and sarcoplasmic proteins, were separated into three fractions and studied with regard to their solubilisation, denaturation and aggregation, degradation and strengthening of protein structures for the three treatments (raw, heated and H-P treated). Measurements included DSC, SDS-PAGE, surface hydrophobicity, and the appearance, length and width of myofibres (light microscopy). For the connective tissue fraction, heat solubility was determined. It is suggested that the mechanism for this improvement in tenderness is the formation of a strengthened myofibrillar structure that, when sheared by mastication, allows the crack to pass through the meat rather than dissipate into a more visco-elastic structure. In this way a more brittle fracture is achieved and the meat is perceived as more tender. The pre-requisite is that adequate enzymatic activity has occurred. It is suggested that cathepsins are responsible.


Subject(s)
Food Handling/methods , Food Technology , Hot Temperature , Meat , Muscle Proteins/chemistry , Muscle, Skeletal/chemistry , Pressure , Animals , Cathepsins , Cattle , Connective Tissue , Cooking/methods , Elasticity , Humans , Mastication , Meat/standards , Myofibrils/chemistry , Protein Denaturation , Sarcoplasmic Reticulum , Solubility , Viscosity
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