Comparative study on degradation, aggregation and rheological properties of actomyosin from cold, temperate and warm water fish species

Bu çalışmada, Alaska pollock (Theragra chalcogramma), Pacific whiting (Merluccius productus), bigeye snapper (Priacanthus spp.), lizardfish (Saurida spp.) ve threadfin bream (Nemipterus spp.) surimilerinden hazırlanan aktomyozinin proteolitik parçalanma ve ısıl topaklanma eğilimi ve reolojik özellikleri karşılaştırmalı olarak incelenmiştir. Arıtılmamış aktomyozin örneklerinde belirgin bir endojen proteolitik aktivite görülürken, Pacific whiting ve lizardfish en yüksek proteolitik aktiviteyi göstermişlerdir. SDS-PAGE analizi, Pacific whiting, bigeye snapper, lizardfish ve threadfin bream miyozin ağır zincir bantlarının yoğunluğunun inkübasyon süresi uzadıkça azaldığını, orta ve düşük molekül ağırlıklı proteinlerin oluştuğunu göstermiştir. Test edilen bütün balık türleri için 0,5°C dk 1 ısıtma hızı daha yüksek bulanıklık değerlerine neden olurken, bunu 1,0°C dk 1 ve daha sonra 2,0°C dk 1 ısıtma hızları izlemiştir. Bulanıklığın artmaya başladığı sıcaklık değeri balık türünden belirgin bir şekilde etkilenmiştir. Aktomyozinin sıcaklık tarama testlerinden elde edilen dinamik depolama modülü pik sıcaklıklarının diferansiyel taramalı kolorimetre geçiş sıcaklık değerlerine yakın olduğu görülmüştür. Bu, dinamik testlerden elde edilen piklerin protein denatürasyon sıcaklıkları ile ilgili olduğuna işaret etmektedir. Düşük ısıtma hızları, ısıl geçiş sıcaklığının daha düşük bir değere kaydırmıştır. Bu sonuçlar, protein jeli oluşum özellikleri ve proteolitik parçalanma açısından balık türlerinin ısıl hassasiyetinin daha iyi anlaşılmasını sağlayacaktır.

Soğuk, ılık ve sıcak su türlerinden elde edilen aktomiyosinin parçalanma, topaklanma ve reolojik özellikleri hakkında karşılaştırmalı çalışma

Proteolytic degradation and thermal aggregation patterns and dynamic rheological properties of actomyosin prepared from Alaska pollock (Theragra chalcogramma), Pacific whiting (Merluccius productus), bigeye snapper (Priacanthus spp.), lizardfish (Saurida spp.) and threadfin bream (Nemipterus spp.) surimi were comparatively studied. There was a significant endogenous protease activity observed in crude actomyosin samples where Pacific whiting and lizardfish exhibited the highest proteolytic activity. SDS-PAGE analysis showed that intensity of myosin heavy chain bands of Pacific whiting, bigeye snapper, lizardfish and threadfin bream decreased with extended incubation time, resulting in medium and low molecular weight proteins. For all tested fish species, a 0.5°C min 1 heating rate resulted in higher turbidity values followed by 1.0°C min 1 and then 2.0°C min 1. Temperature onset point for turbidity increase was significantly affected by species. Storage modulus peak temperatures, obtained from temperature sweep tests of actomyosins, were similar to thermal transition values obtained from differential scanning calorimetry, indicating that peaks obtained from the dynamic tests were related to protein denaturation temperatures. Slower heating rate shifted the thermal transition temperature to a lower value. These observations should give better understanding of the thermal sensitivity of fish species with regards to gelation properties and proteolytic degradation.

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Ahhmed, A.M., Nasu, T., Huy, D.Q., Tomisaka, Y., Kawahara, S. and Muguruma, M. 2009. Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef. Meat Science, 82:170-178.
An, H.J., Seymour, T.A., Wu, J.W. and Morrissey, M.T. 1994a. Assay systems and characterization of Pacific whiting (Merluccius productus) protease. Journal of Food Science, 59:277-281.
An, H.J., Weerasinghe, V., Seymour, T.A. and Morrissey, M.T. 1994b. Cathepsin degradation of Pacific whiting surimi proteins. Journal of Food Science, 59:1013- 1017.
Benjakul, S., Visessanguan, W. and Leelapongwattana, K. 2003a. Purification and characterization of heat-stable alkaline proteinase from bigeye snapper (Priacanthus macracanthus) muscle. Comparative Biochemistry and Physiology B-Biochemistry and Molecular Biology, 134:579-591.
Benjakul, S., Visessanguan, W. and Tueksuban, H. 2003b. Heat-activated proteolysis in lizardfish (Saurida tumbil) muscle. Food Research International, 36:1021-1028.
Chan, J.K. and Gill, T.A. 1994. Thermal aggregation of mixed fish myosins. Journal of Agricultural and Food Chemistry, 42:2649-2655.
Chan, J.K., Gill, T.A. and Paulson, A.T. 1993. Thermal aggregation of myosin subfragments from cod and herring. Journal of Food Science ,58:1057-1061.
Damodaran, S. 1997. Food proteins and their applications. NY: Marcel Dekker Inc, New York 681pp.
Esturk, O., Park, J.W. and Thawornchinsombut, S. 2004. Effects of thermal sensitivity of fish proteins from various species on rheological properties of gels. Journal of Food Science, 69: 412-416.
Fernandez-Martin, F., Perez-Mateos, M. and Montero, P. 1998. Effect of pressure/heat combinations on blue whiting (Micromesistius poutassou) washed mince: thermal and mechanical properties. Journal of Agricultural and Food Chemistry, 46:3257-3264.
Foegeding, E.A., Allen, C.E. and Dayton, W.R. 1986. Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels. Journal of Food Science, 51:104-108.
Gill, T.A., Chan, J.K., Phonchareon, K.F. and Paulson, A.T. 1992. Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin. Food Research International, 25:333-341.
Hastings, R.J., Rodger, G.W., Park, R., Matthews, A.D. and Anderson, E.M. 1985. Differential scanning calorimetry of fish muscle - the effect of processing and species variation. Journal of Food Science, 50:503-506.
Hemung, B.O., Li-Chan, E.C.Y. and Yongsawatdigul, J. 2008. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chemistry, 111:439-446. Hermansson, A.M. 1979. Aggregation and denaturation involved in gel formation. In: A Pour-El, (Ed), Functionality and Protein Structure. American Chemical Society, Washington, DC. 81-103.
Howell, B.K., Matthews, A.D. and Donnelly, A.P. 1991. Thermal-stability of fish myofibrils -a differential scanning calorimetric study. International Journal of Food Science and Technology 26:283-295.
Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227:680 - 685.
Lefevre, F., Culioli, J., Joandel-Monier, S. and Ouali, A. 1999. Muscle polymorphism and gelling properties of myofibrillar proteins from poultry, mammals and fish. In: Y. L., Xiong, C-T., Ho, F., Shahidi, (Eds), Quality Attributes of Muscle Foods. Kluwer Academic/Plenum Publishers, New York. 365391.
Lefevre, F., Fauconneau, B., Thompson, J.W. and Gill, T.A. 2007. Thermal denaturation and aggregation properties of Atlantic salmon myofibrils and myosin from white and red muscles. Journal of Agricultural and Food Chemistry, 55:4761-4770.
Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265- 275.
Park, J.D., Yongsawatdigul, J., Choi, Y.J. and Park, J.W. 2008. Biochemical and conformational changes of myosin purified from Pacific sardine at various pHs. Journal of Food Science, 73:C191-C197.
Park, J.W. and Lanier, T.C. 1989. Scanning calorimetric behavior of tilapia myosin and actin due to processing of muscle and protein-purification. Journal of Food Science 54:49-51.
Poulter, R.G., Ledward, D.A., Godber, S., Hall, G. and Rowlands, B. 1985. Heat-stability of fish muscle proteins. Journal of Food Technology. 20:203-217.
Privalov, P.L. 1982. Stability of proteins - proteins which do not present a single cooperative system. Advances in Protein Chemistry, 35:1-104.
Riemann, A.E., Lanier, T.C. and Swartzel, K.R. 2004. Rapid heating effects on gelation of muscle proteins. Journal of Food Science, 69: 308-314.
Saeed, S. and Howell, N.K. 2004. Rheological and differential scanning calorimetry studies on structural and textural changes in frozen Atlantic mackerel (Scomber scombrus). Journal of the Science of Food and Agriculture, 84:1216-1222.
Sano, T., Noguchi, S.F., Matsumoto, J.J. and Tsuchiya, T. 1990. Effect of ionic-strength on dynamic viscoelastic behavior of myosin during thermal gelation. Journal of Food Science, 55:51-54.
Sano, T., Noguchi, S.F., Tsuchiya, T. and Matsumoto, J.J. 1988. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science, 53:924-928.
Sano, T., Noguchi, S.F., Tsuchiya, T. and Matsumoto, J.J. 1989. Contribution of tropomyosin to fish muscle gel characteristics. Journal of Food Science 54:258-264.
Stone, A.P. and Stanley, D.W. 1992. Mechanisms of fish muscle gelation. Food Research International, 25:381- 388.
Sun, X.D. and Arntfield, S.D. 2011. Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate. Food Chemistry, 124:1011-1016.
Togashi, M., Kakinuma, M., Nakaya, M., Ooi, T. and Watabe, S. 2002. Differential scanning calorimetry and circular dichroism spectrometry of walleye pollack myosin and light meromyosin. Journal of Agricultural and Food Chemistry, 50:4803-4811.
Toyohara, H. and Shimizu, Y. 1988. Relation between the modori phenomenon and myosin heavy-chain breakdown in threadfin-bream gel. Agricultural and Biological Chemistry, 52:255-257.
Xiong, Y.L. and Blanchard, S.P. 1994. Myofibrillar protein gelation - viscoelastic changes related to heating procedures. Journal of Food Science, 59:734-738.
Yongsawatdigul, J. and Park, J.W. 1996. Linear heating rate affects gelation of Alaska pollock and Pacific whiting surimi. Journal of Food Science, 61:149-153.
Yongsawatdigul, J. and Park, J.W. 1999. Thermal aggregation and dynamic rheological properties of Pacific whiting and cod myosins as affected by heating rate. Journal of Food Science, 64:679-683.
Yongsawatdigul, J. and Park, J.W. 2003. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry, 83:409-416.
Yongsawatdigul, J. and Piyadhammaviboon, P. 2004. Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors. Food Chemistry, 87:447-455.