title: Dietary-induced changes of muscle growth rate in pigs: effects on in vivo and postmortem muscle proteolysis and meat quality.
abstract: The effects of various growth rates in pigs induced by four different feeding strategies on the activity of the calpain system and on postmortem (PM) muscle proteolysis and tenderness development were studied. An increased growth rate may be caused by an increased protein turnover, which results in up-regulated levels of proteolytic enzymes in vivo that, in turn, possibly will affect PM tenderness development. It can be hypothesized that increased proteolytic activity pre-slaughter will increase the PM tenderization rate. From postnatal d 28 to d 90 (phase 1) the pigs were divided into two groups, given either ad libitum (A) or restricted (R, 60% of ad libitum) access to feed. The two groups were then divided into two subgroups, given either restricted or ad libitum access to feed from d 91 to slaughter at d 165 (phase 2). Measurements of the activity of mu-calpain, m-calpain, and calpastatin; concentrations of total collagen and the percent of soluble collagen; and RNA, DNA, and elongation factor-2 where made at slaugther. Myofibrillar fragmentation index (MFI) was determined at slaughter and 24 h PM. Warner-Braztler shear force was determined 1 d and 4 d PM. Pigs fed restricted diets in phase 1 and fed ad libitum in phase 2 (RA pigs) had increased growth rates in the last phase compared to pigs fed ad libitum during both phase 1 and phase 2 (AA pigs). The increased growth rate (compensatory growth) was followed by an increased proteolytic potential (mu-calpain:calpastatin ratio), increased MFI values, and higher tenderization rates. There was a positive correlation between the activities of m-calpain and growth rates (r = 0.35, P = 0.03), and between RNA levels and growth rates (r = 0.43, P = 0.006). The proposed hypothesis is largely supported by the results. The activities of both mu- and m-calpain at slaughter were highest in fast-growing pigs. The calpain activity was highest in RA pigs, which in turn also had the fastest growth rates prior tslaughter among the four groups. This implies that the synthesis of these enzymes was up-regulated during the second feeding period to a larger extent in RA pigs. The proteolytic potential and the MFI values indicate that the up-regulated in vivo calpain activity had an effect on PM protein degradation, which also is supported by the higher tenderization rate in RA pigs.
authors.affiliation: Department of Dairy and Food Science, Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark. lak@kvl.dk
authors.forename: L
authors.initials: L
authors.lastname: Kristensen
authors.forename: M
authors.initials: M
authors.lastname: Therkildsen
authors.forename: B
authors.initials: B
authors.lastname: Riis
authors.forename: M T
authors.initials: MT
authors.lastname: Sørensen
authors.forename: N
authors.initials: N
authors.lastname: Oksbjerg
authors.forename: P P
authors.initials: PP
authors.lastname: Purslow
authors.forename: P
authors.initials: P
authors.lastname: Ertbjerg
mesh_terms: D000821:Animal Feed; D000824:Animal Nutritional Physiological Phenomena; D000818:Animals; D002135:Calcium-Binding Proteins / Q000378:metabolism; D002154:Calpain / Q000378:metabolism*; D004038:Diet, Reducing; D005260:Female; D008460:Meat / Q000592:standards*; D018482:Muscle, Skeletal / Q000201:enzymology* / Q000254:growth & development*; D020652:Peptide Elongation Factor 2 / Q000378:metabolism; D011180:Postmortem Changes; D012313:RNA; D013552:Swine / Q000254:growth & development*; D013649:Taste
chemical_list: D002135:Calcium-Binding Proteins; D020652:Peptide Elongation Factor 2; D012313:RNA; C033668:calpastatin; D002154:Calpain