Effect of lactic or acetic acid on degradation of myofibrillar proteins in post-mortem goose (Anser anser) breast muscle

The effects of lactic acid (LA) and acetic acid (AA) on changes in myofibrillar proteins of post-mortem goose breast muscle marinated for 24 h at 5 °C were studied. Purified myofibrils were prepared from 0.1 M LA or AA samples and controls (non-marinated samples) after 0, 1, 3, 7 or 14 days of storage at 5 °C. The changes in myofibrillar proteins of goose muscle were examined by SDS-PAGE. Goose breast muscle marinated in LA and AA exhibited degradation of myosin heavy chains. The appearance of ∼95 and ∼27 kDa components and the disappearance of titin and nebulin were also more rapid than for control muscle. These results suggest that acid marination enhanced the post-mortem proteolysis of goose breast muscle. © 2000 Society of Chemical Industry

[1]  M. Farouk,et al.  Acceptability and functional properties of restructured roast from frozen pre-rigor injected beef. , 1997, Meat science.

[2]  M. Matsuishi,et al.  Proteasome from rabbit skeletal muscle: Some properties and effects on muscle proteins. , 1997, Meat science.

[3]  M. T. Chen,et al.  Acceleration of post-mortem changes in Tsaiya duck (Anas platyrhynchos) breast muscle by lactic acid marination. , 1997, British poultry science.

[4]  I. Beis,et al.  Proteolytic degradation of isolated myofibrils and myofibrillar proteins by m‐calpain from the skeletal muscle of the amphibian Rana ridibunda , 1996 .

[5]  R. Chou,et al.  Post‐mortem Changes in Breast Muscles of Mule Duck , 1996 .

[6]  E. Huff-Lonergan,et al.  Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. , 1996, Journal of animal science.

[7]  R. Chou,et al.  Post‐mortem changes in myofibrillar proteins of breast and leg muscles from broilers, spent hens and Taiwanese Country Chickens , 1994 .

[8]  A. Saunders The effect of acidification on myofibrillar proteins. , 1994, Meat science.

[9]  M. Koohmaraie,et al.  Muscle proteinases and meat aging. , 1994, Meat science.

[10]  C. Ho,et al.  Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. , 1994, Biochimie.

[11]  Matsuishi Masanori,et al.  Mode of action of rabbit skeletal muscle cathepsin B towards myofibrillar proteins and the myofibrillar structure. , 1992 .

[12]  M. Koohmaraie Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization, and comparison of its effects on myofibrils with mu-calpains. , 1992, Journal of animal science.

[13]  M. Farouk,et al.  Post-exsanguination Infusion of Ovine Carcasses: Effect on Tenderness Indicators and Muscle Microstructure , 1992 .

[14]  E. Dransfield Modelling post-mortem tenderisation-III: Role of calpain I in conditioning. , 1992, Meat science.

[15]  M. Koohmaraie,et al.  Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. , 1991, Journal of animal science.

[16]  T. Gibson,et al.  Evidence that nebulin is a protein‐ruler in muscle thin filaments , 1991, FEBS letters.

[17]  J. Fritz,et al.  Changes in Titin and Nebulin in Postmortem Bovine Muscle Revealed by Gel Electrophoresis, Western Blotting and Immunofluorescence Microscopy , 1991 .

[18]  E. D. Strange,et al.  Effects of Lactic Acid on Epimysial Connective Tissues of Muscles Used for Restructured Beef Steaks , 1990 .

[19]  G. C. Arganosa,et al.  Organic Acids as Tenderizers of Collagen in Restructured Beef , 1989 .

[20]  A. F. Anglemier,et al.  Gel electrophoretic analysis of the protein changes in ground beef stored at 2⁰C , 1989 .

[21]  K. Wang,et al.  Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line , 1988, The Journal of cell biology.

[22]  S. M. Wang,et al.  Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin, and myosin , 1988, The Journal of cell biology.

[23]  E. Bandman,et al.  An immunological method to assess protein degradation in post-mortem muscle. , 1988, Meat science.

[24]  A. Ouali,et al.  Comparative action of cathepsins D, B, H, L and of a new lysosomal cysteine proteinase on rabbit myofibrils. , 1987, Meat science.

[25]  E. Kempner,et al.  A physiological role for titin and nebulin in skeletal muscle , 1986, Nature.

[26]  R. Robson,et al.  Effect of Cathepsin D on Bovine Myofibrils under Different Conditions of pH and Temperature , 1986 .

[27]  S. Pemrick,et al.  Qualitative analysis of skeletal myosin as substrate of Ca2+-activated neutral protease: comparison of filamentous and soluble, native, and L2- deficient myosin , 1984, The Journal of cell biology.

[28]  A. F. Anglemier,et al.  Effects of Postmortem Storage on Muscle Protein Degradation: Analysis by SDS‐Polyacrylamide Gel Electrophoresis , 1984 .

[29]  A. Ouali Sensitivity to ionic strength of MgCa-enhanced ATPase activity as an index of myofibrillar ageing in beef. , 1984, Meat science.

[30]  T. Matsumoto,et al.  Mode of degradation of myofibrillar proteins by rabbit muscle cathepsin D. , 1983, Biochimica et biophysica acta.

[31]  K. Wang,et al.  Titin: major myofibrillar components of striated muscle. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[32]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[33]  D. E. Goll,et al.  Determination of proteins in "Tris" buffer by the biuret reaction. , 1968, Analytical biochemistry.