title: The physical and biochemical changes in springbok (Antidorcas marsupialis) Longissimus thoracis et lumborum and Biceps femoris muscle during ageing.
abstract: This study aimed to determine the optimum ageing period for vacuum-packed springbok (Antidorcas marsupialis) Longissimus thoracis et lumborum (LTL) and Biceps femoris (BF) muscle stored at 5.4 ± 1.0°C. Portions of muscle from seven male and six female springbok were aged 1, 2, 5, 8, 14 or 21 days. The Warner Bratzler shear force declined most during the first five days post-mortem (PM), while purge and cooking losses increased significantly with ageing. Calpains I and II and calpastatin activity declined significantly up to five days PM, suggesting that they may be responsible for tenderization. Cathepsins B, BL and H activity increased significantly during ageing. The BF muscle had significantly higher pH, lower purge loss, higher cooking loss, higher WBSF and higher calpain and calpastatin activity than the LTL. No significant differences between the genders or muscles were found for the collagen content or collagen solubility. Springbok LTL and BF muscles should not be aged for longer than five days.
authors.affiliation: Department of Animal Sciences, Stellenbosch University, Private Bag X1, Matieland, Stellenbosch 7602, South Africa.
authors.forename: M K
authors.initials: MK
authors.lastname: North
authors.affiliation: Agricultural Research Council of South Africa, Private Bag X2, Irene 0062, South Africa.
authors.forename: L
authors.initials: L
authors.lastname: Frylinck
authors.affiliation: Department of Animal Sciences, Stellenbosch University, Private Bag X1, Matieland, Stellenbosch 7602, South Africa. Electronic address: lch@sun.ac.za.
authors.forename: L C
authors.initials: LC
authors.lastname: Hoffman
mesh_terms: D000818:Animals; D000866:Antelopes; D002135:Calcium-Binding Proteins / Q000378:metabolism; D002154:Calpain / Q000378:metabolism; D002403:Cathepsins / Q000378:metabolism; D003080:Cold Temperature; D003094:Collagen / Q000378:metabolism; D005260:Female; D005511:Food Handling / Q000379:methods*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008297:Male; D008460:Meat / Q000032:analysis*; D018482:Muscle, Skeletal / Q000201:enzymology / Q000378:metabolism*; D013314:Stress, Mechanical
chemical_list: D002135:Calcium-Binding Proteins; C033668:calpastatin; D003094:Collagen; D002403:Cathepsins; D002154:Calpain
keywords: Calpains; Cathepsins; Conditioning; Game meat; Tenderization