‘THE EFFECT OF CHILLING & FREEZING ON MEAT QUALITY W.F. Spooncer, 0.2. Snith & V.H. Powell CSIRO Meat Research Laboratory Ewmnopuerton Meat quality is usually assessed by consumers in terms of colour, tenderness, juiciness, flavour, fat cover and marbling. These characteristics are influenced by the type and age of livestock used to produce the meat, but can also be very much influenced by processing, resulting in variations in the quality of meat fron similar animals. For example, chilling end freezing affect all the above factors except fat cover and marbling. The relative importance of these factors depends on how the customer intends to use the meat. Butchers prefer to purchase tender meat with good colour, while exporters and manufacturers of smallgoods and hamburgers prefer to use lean meat with high water holding capacity and emulsifying ability. Most of the procedures used by meat processors to control product quality are based on regulations which are mainly concerned with meat preservation. If a meatworks wishes to improve the other attributes of meat quality, e.g. tenderness, then the processing procedures have to be modified. ‘TENDERNESS Apart from fat, the mein structural components of meat are the connective tissue proteins and the contrectile proteins. The tenderness/ toughness of a piece of meat is determined by the condition of these structural proteins. Connective tissue Muscles are not directly attached to the skeletal structure. A complex system of sheaths of connective tissues bind muscle fibres together (Figure 1) and merge with each other at various intervals. ‘They finally blend with the tendons, which enchor the muscles to the bones. Connective tissue is thus an integral part of the musculature of the enimal and therefore must be taken into account vhen discussing properties of muscles. Connective tissue varies in strength depending upon the age of the animal and the part of the animal from which it came, With increasing animal age, connective tissue becomes stronger and more resistant to breakdown during cooking. The amount of connective tissue in different muscles depends on how much work the muscle has to do and how the muscle is attached to the skeletal structure, The nature and distribution of connective tissue has given us our basic knowledge of which muscles we can expect to be tough or tender. For example, we expect yearling or lamb meat to te more tender than ox or hogget. We also expect sirloin to be more tender than chuck from the same animal, because chuck contains more connective tissue than sirloin.SNIBLONd F3113vELWOD ~ 1x51 A936 gf Si SSH. 40 NOLLyNY TAKE Ky ung . “WTSAWOGNA G3TI¥2 ansstL BALLOANNOD 3HL Ag GaSOTONE $i a TIUGIdOAW HOW ATIHM “WOISAWTaag gaTWd anssts SAILOANNOD AHL Ag G3dNNGEUNS ayy SPIGNNG Byqrs © (G3SC"19N3) TOSAW BNL 'STISNW 3HL ONTCNNOYEAS wilt sawtaa aativd RNSSTL AALLS2NNOD 3b SHLV3HS NOTHR SUL OLNT 39UBW CNY 3NOE SHI OL C2LI3NNOD ayy ShodNaL SISA NI 3NssTL BAILIINNOD dO NOLLWuLSniT 1 My wnyskuidy, unishuiopun : sejpung saqia ajasnyai 'T toryContractile proted To appreciate how a muscle contracts and how this affects tenderness we have to look at the fine structure of the muscle tissue. Figure 2 shows sone of the structure of « muscle fibre and how fibres are bound together by connective tissue to make a complete muscle. Single muscle fibres can be seen with the naked eye, as they are about 0.25 mm diameter. A fibre is made up of a bundle of rod sheped microscopic myofibrils which are sheathed in connective tissue. A single myofibril consists of repeating units called sarcomeres. In each sarcomere there are strands of myofibriller proteins and in particular two different protein molecules, actin and myosin. The arrangement of these proteins is shown diagrammatically in Figure 3. To make a muscle contract, these proteins slide in between each other and the sarcomere stortens. In turn, the whole muscle shortens end this contraction in the living animal is translated into bone movement via the connective tissue. As far as meat quality is concerned, a muscle which conteins contracted or shortened sarcomeres is tougher than a relaxed muscle. This is because it becomes progressively more difficult to dite through ‘the increased number of filaments as the sarcomere shortens. In addition, the area of veakness in a sarcomere (the space between the Z-line end the myosin filament) decreases as shortening increases, and more force is necessary to shear through the meat. Tne relationship between percentage shortening of sarcomeres and toughness is shown in Figure hat makes muscle contract? Bnergy is stored by muscles 25 a sugar called glycogen. In a live enimal, glycogen reacts with oxygen to produce carbon dioxide, water and energy in the form of a compound called ATP (adenosine triphosphate). ‘hen @ muscle has to do work, ATP supplies energy directly to the syofibrillar proteins end the myofibrils contract (Figure 5). After the animal is slaughtered the glycogen continues to break down to release energy. Because there is no longer any oxygen available to the muscle, lactic acid is formed instead of water and carbon dioxide. The muscle becomes acidic and the pli (the unit of acid measurement) falls From healthy and rested animals, glycogen gradually breaks down over a period of 48 hours and the pli drops from abcut 7.3 to 5.4-5.6. The rate and extent of this pH change can vary, as shown in Figure 6. When the glycogen is exhausted, the muscle is set in rigor mortis.a ~N ONE SARCOMERE SRTERF SRE COHHECTIVE TISSUE mH FIS. 2 DIAGRAM OF SOME OF THE STRUCTURES WHICH MAKE uP MUSCLE ‘YESsisFEG, 3: MYOSIN ACTIN oe i g 3 = . b~— Al ee SARCONERE SARCOMERE © SARCOMERE STRETCHED WEAR REST © SHORTENED LENGTH RIAGRAM OF THE RELATIVE POSITION OF JHE ACTIN AND AYOSIN PROTEIN in aA SARCOMERE UNIT SHEN STR > AT REST AMD SHORTENEDeee eee _ ey SARCUMERE LENGTH ALOUT 1.3 qa MEAT et a IPEY AGEING { / \ | tereasixe | f : | SHEAR FORCE / | « SARCOMERE LENGTH BELOW i ae 832 MEAT NOTICEABLY, \ dt uMITs) ‘sa a UCT i | ABOUT 2 im ~ ea nccmeraniz 4 | _ oo 4 i I { DERCENT SHORTENING iG: % THCREASE IN YOUCHMESS MIT INCREASED sHoRT! F MEAT (SHEAR Force? awe,g ‘914 poeaNg] ¢ J} DM #4 \@PLXOLp HOg ibo/ snonteane ae, Sionaoud | . aeo3 FE sisym|* HOYSNS] <——— % freee (NOLLVMIIS38) WYWINY SAT NI\ PH \ war Q ee 6 3 @ 2 a 8 pe g ye Time {im sours) POST-MORTEN FIG. 5 TNE CHANGE IN PH VS. TIME POST-HORTEM " FOR ANIMALS IN VARIQUS STATES OF STRESS, i i {\ 30 \ SHORTENING \ & 28 4 % a 30 20 ce at veMPERAruRE (°¢} 3G. F APPROKIMATE RELATIONSHEP BETWEEN PERCENTAGE SHORTENTHG ANS HUSCLE TEMPERATURE PRE-RIGOR2-9 The Effects of Chilling and Freezing Cold shortening One result of this release or cneray after death is that there is a slight increase in muscle temperature. Another effect is that number of the highly valued hindquarter muscles which are free to contract, do so. The amount of muscle contraction or shortening is highly dependent on temperature. The approximate relationship between shortening and temperature in unrestrained pre-rigor muscle is shown in Figure 7. The minimum amount of shortening occurs at about 15°C. ‘The increased amount of shortening vhich occurs below 15°C is called ‘cold! shortening and above 15°C it is called rigor shortening. As a rough guide, meat which cools below 10°C within 10-12 hours after slaughter cold-shortens to the extent thet it is noticeably tough when eaten (hardly any shortening takes place after 12 hours post mortem), Figure § shows a measured cooling rate which resulted in cold shortened meat. Figure 9 shows the anount of shortening which can occur in equivalent pieces of neat passing into rigor at 15°C and 1°C. Once the pH falls below 6.2 there is insufficient energy for the muscle to cold-shorten. Thus for tenderness the surface muscle should not be chilled below 10°C in 10-12 hours end/or should not be chilled below 10°C until the pH is equal to or less than 6.2. ‘Thaw shortening A third type of muscle shortening - thew shortening - can result in more exaggerated muscle contraction and produce tougher meat then either cold or rigor shortening, If a muscle is frozen solid before it is in rigor, the rigidity caused ty freezing prevents the’muscle from shortening, However, if the muscle is thawed rapidly, it may shorten by up to 60-70% of its original length and lese massive amounts of drip. Thaw shortening can be avoided if the meat is thawed slowly (say, at -3°C) because although the chemical changes which cause shortening take place as the meat thaws, the muscle is retrained from shortening because it is still partially frozen. Clearly, any pre- or post-slaughter treatment that allows the muscles of 2 carcass to set in a contracted state will result in tougher meat. A number of procedures have been developed for optimizing tenderness. One such process is 'Tenderstretch', in which beef sides, or mutton and lamb carcasses, arc chilled whilst hung from the pelvic region. This holds many important muscles in a stretched state, preventing them from cold shortening. Another process is ‘ageing’, while a third process ~ electrical stimulation - is discussed in Mr. B.Y, Johnson's Lecture No.3 of the Refrigeration for Meat Industry Engineers Seminar, "Processing Procedures to Achieve Microbiological & Quality Controls".