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Volumn 88, Issue 4, 2004, Pages 543-548

Thermal inactivation characteristics of acid and alkaline phosphatase in fish and shellfish

Author keywords

Acid phosphatase; Alkaline phosphatase; Marine foods; Thermal inactivation

Indexed keywords

ACID PHOSPHATASE; ALKALINE PHOSPHATASE;

EID: 3242734108     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2004.01.069     Document Type: Article
Times cited : (20)

References (29)
  • 1
    • 0032577639 scopus 로고    scopus 로고
    • Purification and characterization of alkaline phosphatase containing phosphotyrosyl phosphatase activity from the bacterium Prevotella intermedia
    • Ansai T., Awano S., Chen X., Fuchi T., Arimoto T., Akifusa S., Takehara T. Purification and characterization of alkaline phosphatase containing phosphotyrosyl phosphatase activity from the bacterium Prevotella intermedia. FEBS Letters. 428:1998;157-160
    • (1998) FEBS Letters , vol.428 , pp. 157-160
    • Ansai, T.1    Awano, S.2    Chen, X.3    Fuchi, T.4    Arimoto, T.5    Akifusa, S.6    Takehara, T.7
  • 3
    • 0042562161 scopus 로고    scopus 로고
    • Thermophysical properties of silver hake and mackerel surimi at cooking temperature
    • Belibagli K.B., Speers R.A., Paulson A.T. Thermophysical properties of silver hake and mackerel surimi at cooking temperature. Journal of Food Engineering. 60:2003;439-448
    • (2003) Journal of Food Engineering , vol.60 , pp. 439-448
    • Belibagli, K.B.1    Speers, R.A.2    Paulson, A.T.3
  • 4
    • 0038504664 scopus 로고    scopus 로고
    • Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish
    • Benjakul S., Chantarasuwam C., Visessanguan W. Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish. Food Chemistry. 82:2002;567-574
    • (2002) Food Chemistry , vol.82 , pp. 567-574
    • Benjakul, S.1    Chantarasuwam, C.2    Visessanguan, W.3
  • 5
    • 0026556919 scopus 로고
    • Phosphatase activity and potassium transport in liposomes with Na+, K(+)-ATPase incorporated
    • Berberianm G., Beauge L. Phosphatase activity and potassium transport in liposomes with Na+, K(+)-ATPase incorporated. Biochimica et Biophysica Acta. 1103:1992;85-93
    • (1992) Biochimica et Biophysica Acta , vol.1103 , pp. 85-93
    • Berberianm, G.1    Beauge, L.2
  • 6
    • 77956925467 scopus 로고
    • Mammalian alkaline phosphatases
    • Boyer D. New York: Academic Press
    • Fernley H.N. Mammalian alkaline phosphatases. Boyer D. The enzymes. Vol. I:1971;417-447 Academic Press, New York
    • (1971) The Enzymes , vol.1 , pp. 417-447
    • Fernley, H.N.1
  • 7
    • 0001358628 scopus 로고
    • Chemical and biological indices in seafood quality
    • H.H. Huss, M. Jacobsen, & J. Liston. Amsterdam: Elsevier
    • Gill T.A. Chemical and biological indices in seafood quality. Huss H.H., Jacobsen M., Liston J. Quality assurence in the fish industry. 1992;337-387 Elsevier, Amsterdam
    • (1992) Quality Assurence in the Fish Industry , pp. 337-387
    • Gill, T.A.1
  • 9
    • 0023069715 scopus 로고
    • Optimization of the determination of muscle acid phosphatase in the post-mortem chicken. Study of the stability of enzyme activity during meat storage at 4°C and -20°C
    • el Hadef el Okki S., Philippon C., Mouthon G. Optimization of the determination of muscle acid phosphatase in the post-mortem chicken. Study of the stability of enzyme activity during meat storage at 4°C and -20°C. Annales de Recherches Veterinaires. 18:1987;73-77
    • (1987) Annales de Recherches Veterinaires , vol.18 , pp. 73-77
    • El Hadef El Okki, S.1    Philippon, C.2    Mouthon, G.3
  • 10
    • 0001559818 scopus 로고
    • Structure of a toxic phospholipid in the northern blenny roe
    • A. Ohsaka, K. Hayashi, Sawai Y. New York: Plenum Press
    • Hatano M., Marumoto K., Hashimoto Y. Structure of a toxic phospholipid in the northern blenny roe. Ohsaka A., Hayashi K., Sawai Y. Animal, plant and microbial toxins. Vol. 2:1976;145-151 Plenum Press, New York
    • (1976) Animal, Plant and Microbial Toxins , vol.2 , pp. 145-151
    • Hatano, M.1    Marumoto, K.2    Hashimoto, Y.3
  • 12
    • 0041758556 scopus 로고    scopus 로고
    • Consideration of critical microorganisms and indicator enzymes in connection with the pasteurization of meat products
    • Incze K., Körmendy L., Körmendy I., Zsanóczay G. Consideration of critical microorganisms and indicator enzymes in connection with the pasteurization of meat products. Meat Science. 51:1999;115-121
    • (1999) Meat Science , vol.51 , pp. 115-121
    • Incze, K.1    Körmendy, L.2    Körmendy, I.3    Zsanóczay, G.4
  • 13
    • 0034399688 scopus 로고    scopus 로고
    • Changes in lysosomal enzyme activities and shear values of high pressure treated meat during ageing
    • Jung S., Ghoul M., de Lamballerie-Anton M. Changes in lysosomal enzyme activities and shear values of high pressure treated meat during ageing. Meat Science. 56:2000;239-246
    • (2000) Meat Science , vol.56 , pp. 239-246
    • Jung, S.1    Ghoul, M.2    De Lamballerie-Anton, M.3
  • 14
    • 0031571648 scopus 로고    scopus 로고
    • Occurrence of para-nitropenyl phosphate-phosphatase with calcineurine-like characteristics in Paramecium tetraurelia
    • Kissemehi R., Treptau T., Kottwitz B., Plattner H. Occurrence of para-nitropenyl phosphate-phosphatase with calcineurine-like characteristics in Paramecium tetraurelia. Archives of Biochemistry and Biophysics. 344:1997;260-270
    • (1997) Archives of Biochemistry and Biophysics , vol.344 , pp. 260-270
    • Kissemehi, R.1    Treptau, T.2    Kottwitz, B.3    Plattner, H.4
  • 15
    • 0036183919 scopus 로고    scopus 로고
    • Changes in acid and alkaline phosphatase activities during the spoilage of raw muscle from horse mackerel Trachurus japonicus and gurnard Le pidotoriga microptera
    • Kuda T., Matsumoto C., Yano T. Changes in acid and alkaline phosphatase activities during the spoilage of raw muscle from horse mackerel Trachurus japonicus and gurnard Le pidotoriga microptera. Food Chemistry. 76:2002;443-447
    • (2002) Food Chemistry , vol.76 , pp. 443-447
    • Kuda, T.1    Matsumoto, C.2    Yano, T.3
  • 17
    • 0034893453 scopus 로고    scopus 로고
    • Acid phosphatase activity and color changes in consumer-style griddlie-cooked ground beef patties
    • Lyon B.G., Davis C.E., Windham W.R., Lyon C.E. Acid phosphatase activity and color changes in consumer-style griddlie-cooked ground beef patties. Journal of Food Protection. 64:2001;1199-1205
    • (2001) Journal of Food Protection , vol.64 , pp. 1199-1205
    • Lyon, B.G.1    Davis, C.E.2    Windham, W.R.3    Lyon, C.E.4
  • 18
    • 0029990066 scopus 로고    scopus 로고
    • Utilization of the bone/liver alkaline phosphatase activity ratio in blood plasma as an indicator of ascorbate deficiency in salmonid fish
    • Matusiewicz M., Dabrowski K. Utilization of the bone/liver alkaline phosphatase activity ratio in blood plasma as an indicator of ascorbate deficiency in salmonid fish. Proceedings of the Society for Experimental Biology and Medicine. 41:1996;43-51
    • (1996) Proceedings of the Society for Experimental Biology and Medicine , vol.41 , pp. 43-51
    • Matusiewicz, M.1    Dabrowski, K.2
  • 19
    • 0012182135 scopus 로고
    • Thermal inactivation characteristics of alkaline phosphatase in ultrafiltered milk
    • Mistry V.V. Thermal inactivation characteristics of alkaline phosphatase in ultrafiltered milk. Journal of Dairy Science. 72:1989;1112-1117
    • (1989) Journal of Dairy Science , vol.72 , pp. 1112-1117
    • Mistry, V.V.1
  • 23
    • 0004275986 scopus 로고
    • T.C. Lanier, & C.M. Lee. New York: Marcel Dekker
    • Okada M. Lanier T.C., Lee C.M. Surimi technology. 1992;3-21 Marcel Dekker, New York
    • (1992) Surimi Technology , pp. 3-21
    • Okada, M.1
  • 25
    • 85005741552 scopus 로고
    • Heat resistant of alkaline phosphatases produced by microorganisms isolated from California Mexican-style cheeses
    • Pratt-Lowe E.L., Geiger R.E., Richardson T., Barrett E.L. Heat resistant of alkaline phosphatases produced by microorganisms isolated from California Mexican-style cheeses. Journal of Dairy Science. 71:1988;17-23
    • (1988) Journal of Dairy Science , vol.71 , pp. 17-23
    • Pratt-Lowe, E.L.1    Geiger, R.E.2    Richardson, T.3    Barrett, E.L.4
  • 26
    • 0029689930 scopus 로고    scopus 로고
    • Alkaline phosphatase activity in Penicillium roqueforti and in blue-veined cheeses
    • Rosenthal I., Bernstein S., Rosen B. Alkaline phosphatase activity in Penicillium roqueforti and in blue-veined cheeses. Journal of Dairy Science. 79:1996;16-19
    • (1996) Journal of Dairy Science , vol.79 , pp. 16-19
    • Rosenthal, I.1    Bernstein, S.2    Rosen, B.3
  • 27
    • 0025074285 scopus 로고
    • Kinetic characteristics of soluble and brush border alkaline phosphatase and sucrase activities in developing rat intestine: Effect of hormones
    • Sandhu M., Mahmood A. Kinetic characteristics of soluble and brush border alkaline phosphatase and sucrase activities in developing rat intestine: Effect of hormones. Indian Journal of Biochemistry and Biophysics. 27:1990;88-92
    • (1990) Indian Journal of Biochemistry and Biophysics , vol.27 , pp. 88-92
    • Sandhu, M.1    Mahmood, A.2
  • 28
    • 0033834668 scopus 로고    scopus 로고
    • Evaluation of spectrophotometric and fluorometric methods for alkaline phosphatase activity determination in ewe's milk
    • Scintu M.F., Daga E., Ledda A. Evaluation of spectrophotometric and fluorometric methods for alkaline phosphatase activity determination in ewe's milk. Journal of Food Protection. 63:2000;1258-1261
    • (2000) Journal of Food Protection , vol.63 , pp. 1258-1261
    • Scintu, M.F.1    Daga, E.2    Ledda, A.3
  • 29
    • 0030265217 scopus 로고    scopus 로고
    • Significance of biogenic amines to food safety and human health
    • Shalaby A.R. Significance of biogenic amines to food safety and human health. Food Research International. 29:1996;675-690
    • (1996) Food Research International , vol.29 , pp. 675-690
    • Shalaby, A.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.