Comparative study on the stability of fish actomyosin and pork actomyosin.

[1]  W. Visessanguan,et al.  Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish (Mulloidichthys martinicus) muscle as influenced by iced storage , 2009 .

[2]  M. Muguruma,et al.  Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef. , 2009, Meat science.

[3]  T. Brenner,et al.  Characterization of fish myosin aggregates using static and dynamic light scattering. , 2009 .

[4]  Keiko Hatae,et al.  Liberation of actin from actomyosin in meats heated to 65°C. , 2009, Meat science.

[5]  E. Li-Chan,et al.  Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. , 2008, Food chemistry.

[6]  Ru Liu,et al.  Role of secondary structures in the gelation of porcine myosin at different pH values. , 2008, Meat science.

[7]  W. Visessanguan,et al.  Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota). , 2008, Food chemistry.

[8]  Ru Liu,et al.  Rheological properties of fish actomyosin and pork actomyosin solutions , 2008 .

[9]  H. Kristinsson,et al.  Conformational and rheological changes in catfish myosin during alkali-induced unfolding and refolding , 2008 .

[10]  K. Hsu,et al.  Changes in conformation and sulfhydryl groups of tilapia actomyosin by thermal treatment , 2007 .

[11]  B. Xie,et al.  Studies on fish and pork paste gelation by dynamic rheology and circular dichroism. , 2007, Journal of food science.

[12]  J. Yongsawatdigul,et al.  Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting , 2007 .

[13]  T. Lanier,et al.  Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization , 2007 .

[14]  Chia-Ling Jao,et al.  Changes in conformation and in sulfhydryl groups of actomyosin of tilapia (Orechromis niloticus) on hydrostatic pressure treatment , 2007 .

[15]  H. Kristinsson,et al.  Effect of pH‐Shift Processing and Surimi Processing on Atlantic Croaker (Micropogonias undulates) Muscle Proteins , 2006 .

[16]  S. Lonergan,et al.  Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelation. , 2005, Meat science.

[17]  Shih-bin Lin,et al.  The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash , 2005 .

[18]  J. Park,et al.  Surimi gelation chemistry. , 2005 .

[19]  H. J. Andersen,et al.  Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment - a low-field NMR study. , 2004, Meat science.

[20]  W. Visessanguan,et al.  Effect of high‐temperature setting on gelling characteristic of surimi from some tropical fish , 2004 .

[21]  J. Yongsawatdigul,et al.  Thermal denaturation and aggregation of threadfin bream actomyosin , 2003 .

[22]  J. Culioli,et al.  Thermal gelation of brown trout myofibrils from white and red muscles: effect of pH and ionic strength , 2002 .

[23]  J. Thompson,et al.  The relationship between tenderness, proteolysis, muscle contraction and dissociation of actomyosin. , 2001, Meat science.

[24]  M. Ogawa,et al.  Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. , 2000, Journal of agricultural and food chemistry.

[25]  Tokuji Watanabe,et al.  Microscopic Observation of "An" Particles Prepared from Phaseolus Group and Their Morphological Changes by Treating with Cellulase , 1992 .

[26]  A. Paulson,et al.  Cross‐Linking of Myosin Heavy Chains from Cod, Herring and Silver Hake During Thermal Setting , 1992 .

[27]  A. Paulson,et al.  Effect of salt concentration and temperature on heat-induced aggregation and gelation of fish myosin , 1992 .

[28]  E. Foegeding,et al.  Effect of Heating Rate on Thermally Formed Myosin, Fibrinogen and Albumin Gels , 1986 .

[29]  Hayakawa Shigeru,et al.  Contribution of Hydrophobicity, Net Charge and Sulfhydryl Groups to Thermal Properties of Ovalbumin , 1985 .

[30]  A. Hermansson.  Aggregation and Denaturation Involved in Gel Formation , 1979 .

[31]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[32]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.