Effect of shrimp head protein hydrolysates on the state of water and denaturation of fish myofibrils during dehydration

ABSTRACT:   To utilize fisheries waste products as food materials with functional properties, shrimp head protein hydrolysates (SHPH) from three species of shrimp, that is, Northern pink shrimp ( Pandalus eous ), Endeavour shrimp ( Metapenaeus endeavouri ) and Black tiger shrimp ( Penaeus monodon ), were produced by enzymatic hydrolysis using endopeptidase derived from Bacillus subtilis and exopeptidase derived from Aspergillus oryzae at a level of 0.1% (w/w). SHPH were rich in protein (90–91%) and amino acids (71–84%) but little fat (0.01–0.02%). The average molecular weight of SHPH was 300–1400. The effect of 5% SHPH (dry basis) addition on the state of water and denaturation of lizard fish myofibrils (Mf) during the dehydration process was evaluated by the desorption isotherm and the Ca-ATPase activity, and compared with the effect of sodium glutamate (Na-Glu). SHPH decreased the water activity and the Ca-ATPase inactivation, and increased monolayer sorbed water and multilayer sorbed water of Mf, although these effects of SHPH were smaller than those of Na-Glu. These findings suggest that the SHPH suppressed dehydration-induced denaturation of myofibrillar protein by stabilizing the hydrated water surrounding myofibrils.     

Comparative study on thermal denaturation modes of myosin in walleye pollack and carp myofibrils as affected by salt concentration

ABSTRACT:   The effect of salt concentration on the thermal denaturation profile of myosin in walleye pollack and carp myofibrils was compared by studying the subfragment-1 (S-1) and rod denaturation rates upon heating. Species-specific denaturation mode observed at 0.1 M KCl was no longer detected when samples were heated above 0.5 M KCl, where S-1 and rod denaturation rates were identical to each other. As the heating of the chymotryptic digest of myofibril formed practically no rod aggregates, S-1 denaturation in a form of myosin was the rate limiting step for rod aggregate formation. As the aggregate formation by rod was remarkably suppressed by lowering the temperature, the free movement of myosin tail upon heating was suggested to play an important role in the rod aggregate formation in a high salt medium.     

液态静高压处理牛羊肌肉显微组织变化研究

本文研究分析了高压处理后的牛羊肌肉的显微组织变化 ,经对压力为 70 0 0 atm,施压介质温度为室温 ,施压持续时间为 2 0 min的处理样品和相应的对照组分别进行了透射电子显微镜观察分析其肌原纤维的显微组织变化。发现高压处理后的牛肉肌节收缩率达 34 .8%羊肉收缩率达 33.3%。同时发现肌原纤维的 I带 ,M线和 Z线处发生明显改变 ,说明这些部位的组成蛋白成分出现胶凝化改变。这一研究结果对于进一步研究高压技术对于肉类的嫩化作用具有很大意义。     

Thermal denaturation and autolysis profiles of myofibrillar proteins of mantle muscle of jumbo squid Docidicus gigas

ABSTRACT:    Jumbo squid was very similar to Japanese common squid in terms of myofibrillar Ca²⁺-, Mg²⁺- and K⁺(EDTA)-ATPase activities. Myofibrils of jumbo squid were significantly stabilized upon addition of Ca²⁺ and destabilized by increasing KCl concentration for heating. Incubation of muscle homogenate of jumbo squid induced a selective cleavage of myosin into two major fragments and the cleavage was inhibited by EDTA. Autolysis was prominent at and above 0.3 M NaCl where myosin filaments dissolve. The enzyme involved in the autolysis was proved to be unstable showing maximal autolysis rate at 25°C. Washing the homogenate partially reduced the autolysis activity.     

Rheological properties and structural changes in steamed and boiled abalone meat

ABSTRACT: Changes in tissue structures, rheological properties, and water content of abalone meat were studied in relation to boiling and steaming time. The adductor muscle of abalone Haliotis discus, which was removed directly from the shell, was boiled or steamed for 1 h, 2 h, and 3 h. When observed under a light microscope and by scanning electron microscopy, structural changes in the myofibrils were greatest in the boiled abalone meat compared with the steamed meat. When heating time was increased from 1 h to 3 h, the instantaneous modulus E ₀ of boiled abalone meat decreased gradually with increased heating time, whereas the E ₀ of steamed abalone meat was reduced when heated for 2 h. When heated for 1 h, the relaxation time of steamed abalone meat was much longer than that of boiled meat. There were no significant changes in the relaxation time of abalone meat among the different boiling times, but the relaxation time of steamed abalone meat was reduced gradually with increasing heating times. The study's results confirmed that the difference in rheological properties between the boiled and steamed meats was due mainly to the denaturation level of myofibrils when heated for 1 h, as well as due to the changes in water and solid content and the manner in which the inner water was exchanged after heating time was increased from 1 h to 3 h.     

Effect of protein hydrolysate from Antarctic krill meat on the state of water and denaturation by dehydration of lizard fish myofibrils

ABSTRACT: To utilize Antarctic krill as functional food, protein hydrolysates were prepared by enzymatic hydrolysis. Their effects on the state of water in myofibrils of lizard fish and dehydration-induced denaturation were compared with those from two species of shrimp, glucose, and sodium glutamate. Peptides are major components in hydrolysates, occupying approximately 85–93% of the total materials. The Antarctic krill protein hydrolysates stabilized the bonding of water molecules, leading to suppressed denaturation of myofibrils during the dehydration process. Similar effects were observed for shrimp protein hydrolysates. The effect of the hydrolysate was less than that by glucose and sodium glutamate.     

超高压处理对绵羊肉嫩化机理的研究

实验研究了超高压处理条件下绵羊肌肉感官特性、显微结构、钙激活酶(Calpains)粗酶活性和剪切力值的变化，并探讨了超高压处理对绵羊肌肉的嫩化机理。超高压处理后绵羊肌肉的感官特性发生变化，随处理压力升高，绵羊肌肉颜色变淡，出现轻微的类似蒸煮的成熟风味。在压力为400 MPa，保压时间为10 min的处理条件下，绵羊肌肉显微组织结构变化明显：肌节收缩，肌原纤维的Z线断裂，M线降解，I带变白。当压力水平在100～400 MPa范围变动时，随压力升高，Calpains粗酶活性显著下降(P＜0.01)；当压力达到400 MPa时，Calpains粗酶活性几乎失活。超高压处理后绵羊肉的剪切力值显著下降(P＜0.05)。实验结果表明，超高压处理促进了绵羊肉的嫩化。     

Denaturation mode of carp myofibrils when affected by temperature and salt concentration

ABSTRACT: Heating temperatures of 30–40°C and KCl concentrations of 0.1–0.5 M altered the denaturation mode of carp myofibrils. In 0.1 M KCl medium, heating temperature affected the denaturation of rod more significantly than of subfragment-1 (S-1), and a slow decrease in solubility at 30°C was accompanied by a slow denaturation of rod. KCl concentration at heating altered the denaturation mode differently at 30°C and 40°C. Increased KCl concentrations for heating reduced the rod denaturation rate at 40°C, but it was increased at 30°C. At concentrations above 0.3*Τ*M KCl, the denaturation rate for rod became identical to that for S-1 at both temperatures. Upon heating of chymotryptic digest of myofibrils, S-1 denaturation was similarly detected as in intact myofibrils, whereas practically no rod denaturation was detected. Thus, it was concluded that myosin structure connecting S-1 and rod has an important role in the denaturation process.     

鳙肌原纤维三聚磷酸盐水解酶(TPPase)的活性

采用离子色谱方法检测添加的三聚磷酸盐（STPP）在新鲜碎鳙肉和鳙肌原纤维蛋白中Mf）所发生的水解。研究结果表明，添加到新鲜碎鳙肉中的STPP能被水解成焦磷酸盐（PP）和单磷酸盐（Pi），所生成的PP继续水解，最终产物为Pi。鳙肌原纤维蛋白具有三聚磷酸盐水解酶（TPPase）活性，能将STPP水解成PP和Pi。鳙肌原纤维蛋白TPPase水解STPP的最适温度为25 ℃，最适pH为5.5。低浓度的Mg²⁺能够激活鳙肌原纤维蛋白TPPase ，但Mg²⁺超过5 mmol·L^-1时却起到了抑制作用。鳙肌原纤维蛋白TPPase活性受到KCl的影响，在0.3 mol·L^-1 KCl 条件下活性最高。EDTA-Na₂能够抑制鳙肌原纤维蛋白TPPase活性。