Characterization of a crude lysosomal extract from bovine spleen for its use in the processing of muscle foods

Food Biotechnology

Volumn 12, Issue 3, 1998, Pages 239-262

  Melendo, J A ^a   Beltran J A ^a   Roncales P ^a  

^a UNIVERSITY OF ZARAGOZA   (Spain)

Author keywords

Cathepsins; Collagen; Enzymes; Muscle food; Myofibrillar proteins; Proteases; Spleen

Indexed keywords

ACID LIPASE; CASEIN; CATHEPSIN; CENTRIFUGATION; COLLAGEN; ENZYME ACTIVITY; ESTERASE; FOOD PROCESSING; FOOD PRODUCT; MYOSIN; PEPTIDASE; PEROXIDASE; PROTEIN HYDROLYSIS;

EID: 0032435154     PISSN: 08905436     EISSN: None     Source Type: Journal    
DOI: 10.1080/08905439809549955     Document Type: Article

References (62)

1. Agarwal, K. S. 1990. Proteases cathepsins, a view. Biochem. Educ., 18: 67-72.
2. Antequera, T., López-Bote, C., Córdoba, J.J., García, C., Asensio, M.A. & Ventanas, J. 1992. Lipid oxidative changes in the processing of Iberian pig ham. Food Chem. 45: 105-109.
3. Artigas, G., Sárraga, C. & García-Regueiro, J. A. 1996. Purification process to obtain cathepsin D, B, and L suitable to be used in food industry. Food Biotechnol., 10: 41-54.
4. Asghar, A. & Bhatti, A. R. 1987. Endogenous proteolytic enzymes in skeletal muscle: their significance in muscle physiology and during postmortem aging events in carcasses. Advances Food Res., 31: 343-451.
5. Barrett, A. J. 1970. Cathepsin D: Purification of isoenzymes from human and chicken liver. Biochem. J., 117: 601-607.
6. Barrett, A. J. 1972. Lysosomal enzymes. In: A laboratory handbook. Dinge, J.T. eds. North-Holland Publishing Co. Amsterdam, pgs. 46-135.
7. Barrett, A. J. 1981. Cathepsin G. Methods in Enzymology, 80: 561-565.
8. Barrett, A. J. & Kirschke, H. 1981. Cathepsin B, cathepsin H and cathepsin L. Methods in Enzymology, 80: 535-561.
9. Béchet, D., Obled, A. & Deval, C. 1986. Species variations amongst proteinases in liver lysosomes. Biosci. Rep., 6: 991-997.
10. Beltrán, J.A., Bonnet, M. & Ouali, A. 1992. Comparative action of cathepsins B and L on intramuscular collagen as assessed by differential scanning calorimetry. Meat Sci., 32: 299-306.
11. Beltrán, J.A., Galán, J., Jaime, I. & Roncalés, P. 1994. Action of cathepsin B on intramuscular collagen under conditions simulating conventional aging of meat. A calorimetric study. Sci. Alim. 14: 523-528.
12. Bergman, I. & Loxley, R. 1970. The determination of hydroxiproline in urine hydroxilates. Clin. Chim. Acta, 27: 347-349.
13. Bernal, V.M. & Stanley, D.W. 1986. Changes in the melting characterics of bovine tendon collagen induced by a bacterial collagenase. J. Food Sci. 51: 834-837.
14. Burnette, F.S. 1977. Peroxidase and its relationship to food flavor and quality: a review. J. Food Sci., 42: 1-6.
15. Ceña, P., Jaime, I., Beltrán, J.A. & Roncalés, P. 1992. Proteolytic activity on myofibrils of isolated lamb calpains under conditions of pH, calcium concentration and temperature existing in postmortem muscle. Z. Lebensm. Untersuch. Forsch. 194, 248-251.
16. Cohen, S. H., Kostick, J. A., Robbins, F. M., Segars, R. A. & Walker, J. E. 1979. Action of spleen extract on stored pre-cooked freeze-dried beef. J. Food Sci., 48: 1117-1120.
17. Dayton, W.R., Goll, D.E., Zeece, M.G., Robson, R.M. & Reville, W.J. 1976. A calcium-activated protease possibly involved in myofibrillar protein turnover. I. Purification from porcine muscle. Biochemistry 15: 2150-2158.
18. De Duve, C., Pressman, R., Gianetto, R., Wattiaux, R. & Applemans, F. 1955. Tissue fractionation studies. 6. Intracellular distribution pattern of enzymes in rat-liver extract. Biochem. J., 60: 604-617.
19. Dean, R. T. & Barrett, A. J. 1976. Lysosomes. Essays Biochem., 12: 1-40.
20. Deval, C. H., Bechet, D., Obled, A. & Ferrara, M. 1990. Purification and properties of different isoforms of bovine cathepsin B. Biochem. Cell Biol., 68: 822-826.
21. Doi, E., Shibata, D. & Matoba, T. 1981. Modified colorimetric ninhydrin methods for peptidase assay. Anal. Biochem., 118: 172-184.
22. Ducastaing, A. & Etherington, D. J. 1978. Purification of bovine spleen collagenolytic cathepsin (cathepsin N). Bioch. Soc. Trans., 6: 938-940.
23. Dufour, E., Obled, A., Valin, C., Béchet, D., Huet, J. L. & Ribadeau-Dumas, B. 1987. Purification and aminoacid sequence of chicken liver cathepsin L. Biochemistry, 26: 5689-5695.
24. Eino, M. F. & Stanley, D. W. 1973a. Catheptic activity, textural properties and surface ultrastructure of post-mortem beef muscle. J. Food Sci., 38: 45-50.
25. Eino, M. F. & Stanley, D. W. 1973b. Surface ultrastructure and tensile properties of cathepsin and collagenase treated muscle fibers. J. Food Sci., 38: 51-55.
26. Etherington, D. J., Taylor, M. A. J. & Dransfield, E. 1987. Conditioning of meat from different species. Relationship between tenderising and the levels of cathepsin B, cathepsin L, calpain I, calpain II and ß-glucuroniodase. Meat Sci., 20: 1-18.
27. Etherington, D. J., Taylor, M. A. J., Wakefield, D. K., Cousins, A. & Dransfield, E. 1990. Proteinase (cathepsin B, D, L and calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle. Meat Sci., 28: 99-109.
28. Evans, W. H. 1991. Organelles and membranes of animal cells. In: Biological membranes, Findlay, J.B.C. & Evans, W.H. eds. IRL Press. Oxford, pgs. 1-23.
29. Flores, M., Aristoy, M. C. & Toldrá, F. 1993. HPLC purification and characterization of porcine muscle aminopeptidase B. Biochimie, 75: 861-867.
30. Goll, E. D., Otsuka, Y., Nagainis, P. A., Shannon, J. D., Shate, S. K. & Muguruma, M. 1983. Role of muscle proteinases in maintenance of muscle integrity and mass. J. Food Biochem., 7: 137-177.
31. Imanaka, T., Muto, K., Ohkuma, S. & Takano, T. 1981. Purification and properties of rabbit liver acid lipase (4-methylumbelliferyl oleate hydrolase). Biochim. Biophys. Acta, 665: 322-330.
32. Imanaka, T., Muto, K., Ohkuma, S. & Takano, T. 1984. Characterization of lysosomal acid lipase purified from rabbit liver. Biochem. J., 96: 1089-1101.
33. Kirschke, H. & Barrett, A. J. 1987. Chemistry of lysosomal proteases. In: Lisosome: their role in protein breakdown. Glaumann, H. & Ballard F.J. eds. Academic Press, New York. pgs. 193-238.
34. Kirschke, H., Wood, L., Roisen, F. J. & Bird, W. C. 1983. Activity of lysosomal cysteine proteinase during differentiation of rat skeletal muscle. Biochem. J., 214: 871-877.
35. Kirschke, H., Wiederanders, B., Bröme, D. & Rinne, A. 1989. Cathepsin S from bovine spleen. Biochem. J., 264: 467-473.
36. Koohmaraie, M., Whipple, G., Kretchmar, D. H., Crouse, J. D. & Hersmam, H. J. 1991. Postmortem proteolysis in longisimus muscle from beef, lamb and pork carcasses. J. Anim. Sci., 69: 617-624.
37. Kopp, J. & Bonnet, M. 1982. Qualités des viandes de taurillons: évolution avec l'âge des caractéristiques physico-chimiques des muscles. Le tissu conjonctif musculaire. Bull. Techn. CRZV Theix, INRA, 48: 34-36.
38. Kopp, J., Bonnet, M. & Renou, J. P. 1989. Effect of collagen crosslinking on collagen water interactions (a DSC investigation). Matrix, 9: 443-450.
39. Lardeux, B., Gouhot, B. & Forestier, M. 1983. Improved recovery of rat liver fractions enriched in lysosomes by specific alteration of the sedimentation properties of mitochondria. Anal. Biochem., 131: 160-165.
40. Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. 1951. Protein measurement with folin-phenol reagent. J. Biol. Chem., 193: 265-275.
41. Maciewicz, R. A. & Etherington, J. D. 1988. A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen. Biochem. J., 256: 433-440.
42. Marshall, M. & Chism, G. W. 1979. A comparison of the suitability of three hydrogen donors in the determination of peroxidase activity. J. Food Sci., 44: 942-943.
43. Melendo, J.A., Beltrán J.A. & Roncalés, P. 1998. Tenderization of squid (Loligo vulgaris and Illex coindetti) with bromelain and a bovine spleen lysosomal-enriched extract. Food Res. Int., 30: 335-341.
44. Mikami, M., Whiting, A. H., Taylor, M. A. J., Maciewicz, R. A. & Etherington, D. J. 1987. Degradation of myofibrils from rabbit, chicken and beef by cathepsin L and lysosomal lysates. Meat Sci., 21: 81-97.
45. Motilva, M. J. & Toldrá, F. 1993. Effect of curing agents and water activity on pork muscle and adipose subcutaneus tissue lipolytic activity. Z. Lebensm. Unters. Forsch., 196: 228-232.
46. Nakamura, N., Tsuru, A., Hirayoshi, K. & Nagata, K. 1992. Purification and characterization of vimentin-specific protease in mouse myeloid leukemia cells. Eur. J. Biochem., 205: 947-954.
47. Nomenclature Committee of the International Union of Biochemistry 1984. Enzyme Nomenclature, Academic Press, London.
48. Okitani, A., Matsuishi, M., Matsumoto, T., Kamoshida, E., Sato, M., Matsukura, U., Watanabe, M., Kato, H. & Fujimaki, M. 1988. Purification and some properties of cathepsin B from rabbit skeletal muscle. Eur. J. Biochem., 171: 377-381.
49. Olson, D. G., Parrish, F. C. & Stromer, M. H. 1976. Myofibril fragmentation and shear resistance of three bovine muscles during postmortem storage. J. Food Sci., 41: 1036-1041.
50. Quass, D. W. & Briskey, E. J. 1968. A study of certain properties of myosin from skeletal muscle. J. Food Sci., 33: 180-187.
51. Rico, E., Toldra, F. & Flores, J. 1991. Assay of cathepsin D activity in fresh pork muscle and dry cured ham. Meat Sci., 29: 287-293.
52. Robbins, H. F. & Cohen, S. H. 1976. Effects of the catheptic enzymes from spleen on the microstructure of bovine semimembranosus muscle. J. Text. Stu., 7: 137-142.
53. Robbins, H. F., Walker, J. E., Cohen, S. H. & Chatterjee, S. 1979. Action of proteolytic enzymes on bovine myofibrils. J. Food Sci., 44: 1672-1678.
54. Roncalés, P., Geesink, G., Van Laack, R.L.J.M., Jaime, I., Beltrán, J.A., Barnier, V. & Smulders, F.S.M. 1995. Meat tenderisation: enzymatic mechanisms. In: Expression of tissue proteinases and regulation of protein degradation as related to meat quality". Ouali, A., Smulders, F.S.M. and Demeyer, D. eds. ECCEAMST. Utrecht, pgs. 311-332.
55. Sancho, R, Jaime, I., Beltrán, J.A. & Roncalés, P. 1997. Actin degradation by cathepsins in beef fibers stored at high temperature. J. Muscle Foods, 8: 137-146.
56. Sárraga, C., Gil, M. & García-Regueiro, J. A. 1993. Comparison of calpain and cathepsin (B, L and D) activities during dry-cured ham procesing from heavy and light large white pigs. J. Sci. Food Agric., 62: 71-75.
57. Starkey, P. M. & Barrett, A. J. 1976a. Neutral proteinases of human spleen. Biochem. J., 155: 255-263.
58. Starkey, P. M. & Barrett, A. J. 1976b. Human cathepsin G. Catalytic and inmunological properties. Biochem. J., 155: 264-273.
59. Stead, D. 1983. A fluorimetric method for the determination of Pseudomonas fluorescens Ar11 lipase in milk. J. Dairy Res., 50: 491-502.
60. Takahashi, T. & Tang, J. 1981. Cathepsin D from porcine and bovine spleen. Methods in Enzymology, 80: 565-581.
61. Wiederanders, B., Broemme, D., Kirschke, H., Kalkkinen, N., Rinne, A., Paquette, T. & Toothman, P. 1991. Primary structure of bovine cathepsin S. FEBS Lett., 286: 189-192.
62. Xin, X.Q., Gunesekera, B. & Mason, R.W. 1992. The specificity and elastinolytic activities of bovine cathepsins S and H. Arch. Bioch. Biophys., 299: 334-339.