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The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products

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The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products Food Structure Volume 8 Number 1 Article 17 1989 The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products Gerald Offer Peter Knight Robin Jeacocke Richard Almond Tony Cousins See next page for additional authors Follow this and additional works at: https://digitalcommons.usu.edu/foodmicrostructure Part of the Food Science Commons Recommended Citation Offer, Gerald; Knight, Peter; Jeacocke, Robin; Almond, Richard; Cousins, Tony; Elsey, John; Parsons, Nick; Sharp, Alan; Starr, Roger; and Purslow, Peter (1989) "The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products," Food Structure: Vol. 8 : No. 1 , Article 17. Available at: https://digitalcommons.usu.edu/foodmicrostructure/vol8/iss1/17 This Article is brought to you for free and open access by the Western Dairy Center at DigitalCommons@USU. It has been accepted for inclusion in Food Structure by an authorized administrator of DigitalCommons@USU. For more information, please contact [email protected]. The Structural Basis of the Water-Holding, Appearance and Toughness of Meat and Meat Products Authors Gerald Offer, Peter Knight, Robin Jeacocke, Richard Almond, Tony Cousins, John Elsey, Nick Parsons, Alan Sharp, Roger Starr, and Peter Purslow This article is available in Food Structure: https://digitalcommons.usu.edu/foodmicrostructure/vol8/iss1/17 FOOD MICROSTRUCTURE, Vol. 8 (1989) , pp. 151- 170 0730- 5419/89$3 .00+. 00 Scanning Microscopy International, Chicago CAMF O'Hare) , IL 60666 USA THE STRUCTURAL BASIS OF THE WATER-HOLDIN G, APP EAR AN CE AND TOUGHNESS OF MEAT AND MEAT PRODUCTS Gerald Offer. Peter Knight, Rob1 n Jeacocke, Richard Almond, Tony Cousins. John Elsey, Nick Parsons. Alan Sharp , Roger Starr and Pete r Purslow Mus cle Biology Department, AFRC Inst1tute of Food Research - Bristol Laboratory Langford , Bristol, BS18 7DY, UK Abstract Introduction A structural approach greatly clarifies which In Western societies a larger amount is spent components of meat are responsible for its on meat and meat products than on any other food. tenderness, water-holding and appearance, and the and meat foods present a part i cu l a rl y wide events occurr1 ng during processing. variety of problems and challenges . Structural In living muscle, water is held in the spaces investigations on meat are very helpful because between the thick and thin filaments. Changes in by identifying the spatial arrangement of the content and distribution of water within meat components. they can identify the component originate from changes in this spacing. responsible for a problem affecting meat quality Myofibrils shrink laterally post mortem . The and greatly clarify the mechanism responsible. fluid expelled accumulates between fibre bundles These problems are caused by rather subtle and between fibres and is drain ed by gravity c hanges in the colloidal character of meat and, forming drip. In pale, soft and exudative meat, although much is known about the factors shrinkage of the myosin heads on denaturation producing them, the exact nature of these changes increases myofibrillar shrinkage. In salt has until recently eluded a precise description; solutions used in meat processing, myofibrils only now are meat scientists beginning to explain swell laterally taking up water, probably by an them. We are fortunate in being able to draw on entropic mec hanism. a very large amount of structura l and biochemical The co lour of meat is determined by light infonnation provided by basic biological research scattering as well as by absorption . The light on muscle and connective tissue. We are also scatterers in meat are observed by scanning fortunate 1n that muse 1e ce 11 s are very regular confocal light microscopy to be smaller than 1 ~m and this facllltates both the study of their and concentrated in the A-band regions. 1t is structure and thinking about mechanisms . proposed that 1 ight scattering arises from the In this brief review we have selected three gaps between myofibri 1 s. topics, water-holding, appearance and texture . The structur es responsible for the toughness All levels of structure are informative, from of cooked meat have been studied by observing its single protein molecules up to coarser features fracture behaviour. The perimysial connective that can be seen by eye . Correspondingly, a tissue determines the breaking strength when the number of complementary structural techniques is meat is pulled apart transversely. In proving valuable, including X-ray diffraction, longitudinal tensile tests, the initial event is scanning and transmission electron microscopy, the debonding of fibre bundles from the phase- cont rast, fluorescence, pol ar1 sing, dark­ perimysium so that they contribute independently field and scanning confocal light microscopy . to load-bearing. At greater ex t ensions. it seems likely that fibre bundles progressively fail The Structure of Mus cle leaving perimysial strands as the last structure to break. With aged muscle, the muscle fibres Before considering these three quality probably fail at smaller extensions and therefore attributes, we will first briefly review the contribute less to the breaking strength. structure of muscle (for detailed recent reviews see Squire and Vi bert, 1987). Surrounding each Initial paper received February 5, 1989 muscle is a thick connective tissue sheath, the Manuscript received May 28, 1989 epimysit.rn, which is continuous with the tendon Direct inquiries to G. Offer (Figure 1}. The muscle is divided tnto muscle Telephone number: 44 -934 852 661 fibre bundles by the perimysial connective tissue network. The coarse or primary perimysial network, which is very obvious to the eye, is Key Words: Muscle, meat, light microscopy, further sub~divided by thinner sheets of confocal microscopy, electron microscopy, water­ perimysial connective tissue. typically defining holding, appearance, colour. toughness. texture. a bundle of muscle fibres of the order of 1 1m1 151 G. Offer et al. penmys10l network muscle fibre endomys1al network 1 0 1 ~ ~~~~tuJ ina 1Trsaencs;iiosns t hnro~ g~ctfr0:g ~~~'i~~~lp~u~~ l: 1 1 9 3 0 0 showing the striated appearance. The lower ~~;\;tea 1 .mus~~~rs:ho~~~~c \u:ea c~~n e c t ~~:t \ tss~~ diagram schematically shows how the striations of tracts of muscle. Top, whole muscle; bottom, a the myofibrils are caused by the orderly packing fibre bundle. (Adapted f r om Purslow (1987) by of thick and thin filaments. The A-band is 1.6 ~ m permission of von Nostrand Reinhold Company) . long . {Rep r oduced by pennission of Or Craig and the Longman Group) . are separated f r om one anothe r by t he endomys ial connect i ve ti ssue network. {Figure 1) . The musc l e fibres a re multi nucleated cells, typically 10 to 100 ~ m wide and as much as several centimetres long . They are filled with myofi bri 1 s, the contractile apparatus of muscle . These are long , thin ( 1 to 2 ~m), roughly cylindrical organelles packed side by side {Figure 2) . In white f ibres , whi c h are used for bursts of activity, few mitochondria are present and the myofibrils are separated only by the calcium-stor ing membrane-lined channels of the sarcoplasmic reticullxn . ln red fibres, which are used for sustained or repetitive activity, mitochondria also intrude between adjacent myofi bri 1 s . Myofibrils have a regular striated appearance and, because they are packed in register, the whole muscle f i bre appears striated (Figure 3) . The wi de protei n- dense bands are cal l ed A-ba nds and each has a l i ghter zone, t he H-zone , i n i t s centr al part. In t he middle of t he A-band i s a ~. Scanning el ectron mi crograph of an dense l i ne, t heM-l i ne . The lighter bands a r e ~ cut surface of beef sternomandibular1s called I- bands and each is bisected by a Z-d i sc. muscle. The fibre direction is from left to The stri ations of the myofibril arise because the right . In the two fibres near the surface the myofibril is made up of overlapping arrays of two enclosing endanysial sheaths have been largely kinds of filaments, thick and thin , which fonn a removed revealing the closely packed arrangement repeating pattern {Figure 3}. In transverse of myofibrils within them. Ba r = 20 ~m . sections through the region of overlap, the filaments may be seen to lie in a well-order ed hexagonal lattice (see Figure 4). Each thick across. The collagen fibres in the perimyshrn filament , which is 1.6 lAm long, 1s made up are crimped and arranged in a criss-cross lattice principally of about 300 molecules of the protein (Rowe, 1974). In muscle at rest length, the myosin . The myosin molecule has a long tail collagen fibres in the pe r imysium are arranged at (156 nm x 2 nm wide) at one end of which two an angle of about + 55° t o the muscle fibre axis curved pea r- shaped heads ( 19 nm long) are but asstllle larger Or smaller angles as the muscle flexibly attached (see Figure 6). In the thick shortens or lengthens . I ndividual muscle fibres fi 1 ament t he tai 1 s pack together to form t he 152 Water-hold ing, appearance and toughness of meat shaft, the tails in the two halves pointing in opposite directions. This leaves the heads on the surface where they can interact with the thin fi 1 ament (see Figure 6c) • The thin fi 1 ament is made up principally of about 400 molecules of actin, the precise number depending on the species. Each actin molecule is dliTlb - bell-shaped and can bind one my as in head . The actin molecules pack. in a helical manner with the long axis of each dumb-bell perpendicular to the filament axis .
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