Inhibition of Protease Activity in Muscle Extracts and Surimi from Pacific Whiting, Merluccius productus, and Arrowtooth Flounder, Atheresthes stomias

Muscle extracts of Pacific whiting, Merluccius productus, and arrowtooth flounder, Atheresthes stomias, were assayed for proteolytic activity using azocasein as a substrate. Pacific whiting extracts showed maximum activity at pH 5.0-5.2 and a temperature of 50°C, while arrowtooth flounder extracts had maximum activity at pH 5.5 and 55°C. Three sources of inhibitors (potatoes, egg white, beef plasma protein) were evaluated in vitro for inhibition of protease activity. All three were found to be effective inhibitors in crude muscle extracts. Further studies utilizing these inhibitors in surimi showed that potato was equivalent to both egg white and beef plasma protein in preserving the gel forming characteristics ofheated kamaboko in both species.

Determination of ubiquinone and tocopherol in heart, liver and muscle tissues of fresh water fish, Rohu (Labeo rohita, Hamilton)

The liver, heart and muscle tissues of Rohu, (Labeo rohita, Hamilton) were examined for their ubiquinone (UQ) and tocopherol contents. These three tissues contained respectively 11.60, 3.94 and 0.19 mg of ubiquinone and 10.16, 5.32 and 3.58 mg of tocopherol per 100 g. The 4% (V/V) of diethyl ether (EE) in light petroleum ether (PE) fractions of all three tissues on paper chromatographic separation gave spots having the same Rf value as standard ubiquinone-50 (UQ 10). Both the 4% and 6% (V/V) diethyl ether in light petroleum ether fraction of liver, heart and muscle tissues gave a single spot with the same Rf value as α – tocopherol.

Postmortem changes in hilsa fish. Pt. 1. Studies on rigor-mortis, typical yields and protein composition of dark and white muscle of hilsa fish (Tenualosa ilisha Ham.)

Hilsa (Hilsa ilisha) caught by gill net were immediately killed by cranial spiking. Three fish were kept in ice (0°C) and three other at room temperature (33°C) to follow development of rigor mortis and changes in muscle pH. The rest were frozen stored at -20°C. Rigor started 15 minutes after death in all fish and reached full rigor (100%) state in 2 and 4 hours respectively in fish kept at 33° and 0°C. The fish at 33°C deteriorated 16 hours after while in full rigor but those at 0°C lasted 26 hours of death without deterioration. Freshly caught hilsa had a muscle pH around 7 which decreased with time rapidly at 33°C and slowly at 0°C. The relative proportion of protein fraction in white and dark muscle of fish stored at 0°C and -20°C were also studied. The proportion of dark muscle was 30.34% of the white muscle. White muscle in fish at 0°C was found to contain 32.0% sarcoplasmic, 57.6% myofibrilla, 9.4% alkali-soluble and 1.1% stroma protein whereas these proteins in dark muscle were 29.9%, 58.4%, 9.8% and 1.9% respectively. The protein fractions of white muscle in frozen-fish were found 27.6% sarcoplasmic, 64.7% myofibrilla, 6.0% alkali-soluble and 1.7% of stroma protein whereas they were 30.6%, 58.6%, 8.9 and 1.9% for dark muscle. Some changes occurred in protein composition during frozen storage. The relative amounts of sarcoplasmic, alkali soluble and stroma protein fractions decreased while myofibrilla fraction increased in frozen condition. This may be attributed to drip loss of soluble protein during thawing.

Comparison of physicochemical properties of muscle proteins in cultured and wild prawns (Penaeus (Fenneropenaeus) orientalis Kishinouye, 1918)

Protein physicochemical properties in cultured and wild prawns (Penaeus (F.) orientalis Kishinouye, 1918) were studied and compared. Protein fractions were separated into water-soluble, salt-soluble, alkali-soluble, and stroma. The results showed that salt- and alkali-soluble proteins were slightly higher in wild prawns and water-soluble proteins were higher in cultured prawns. There were only slight differences in Ca2+-ATPase, MG2+-ATPase, and ATP sensitivities. The textural values of wild prawns were significantly higher than the cultured ones.

Effect of electric stimulation on heart beat and body muscle in fish

The effect of AC and DC electric stimulations on the heart-rate and the entire body of Heteropneustis fossillis, Tilapia mossambica and Macrobrachium rosenbergii were studied and presented in kymograph tracings. The reaction of spinal cord in Puntius ticto, Heteropneustis fossilis and Tilapia mossambica to D. C. field was observed to find out its role in electric shocks. A test-check of the electrical resistance of a few species was also conducted. The effect of D. C. and A.C. on the body muscle was found to be the same as that in the case of frog. Different degrees of cardiac slowing were observed in AC and DC. Unbalanced galvanotropic movements were also noticed in spinal fishes.

Purification and properties of Aspartate aminotransferase (E.C. 2.6.1.1) from skeletal muscle of Cirrhina mrigala

Aspartate aminotransferase (E.C. 2.6.1.1.) from the skeletal muscle of fresh water fish Cirrhina mrigala has been purified 40 fold by ammonium sulphate fractionation, adsorption on alumina Csub(8) gel and chromatography using DEAE-cellulose column and the properties of the purified enzyme studied. The pH optimum of the enzyme is 7.8. The Km value of aspartic acid and 2-oxoglutaric acid are found to be 2.8 x 10sub(-3) M and 1.0 x 10sub(-4) M respectively. The activity of enzyme is inhibited by p-chloromercurybenzoate, hydroxylamine hydrochloride and sodium cyanide. The inhibition by pchloromercurybenzoate is reversed by reduced glutathione, B-mercaptoethanol and cysteine. Dicarboxylic acids such as maleic acid, malic acid and succinic acid inhibit the enzyme activity. The enzyme is not activated by any of the metal ions tested and heavy metal ions such as mercury and silver strongly inhibit the enzyme activity.

Freeze drying of fishery products: Part IV - Biochemical changes occurring in prawn muscle during freezing, freeze drying and prolonged storage of the freeze dried product

The changes occurring in water and salt extractable protein and non-protein fractions in prawn muscle of different species during freezing, freeze drying and subsequent prolonged storage have been studied. There is no denaturation of water extractable proteins, whereas salt extractable proteins were rendered insoluble to the extent of 21% due to freeze drying. The freeze dried products remained in good edible condition for 32 months of storage up to which storage characteristics were followed.

Some physical properties of the muscle lipid of two freshwater teleosts, Ophicephalus striatus (Bloch.) and Clarias batrachus (Linn.)

Various physical properties (viscosity, fluidity, surface tension and specific gravity) have been determined for muscle lipids of Ophicephalus striatus and Clarias batrachus. Results are presented and the methods used in determination noted. The physical parameters studied are found to be species-specific.

Purification and characterisation of phosphorylase from muscle of Tilapia (Tilapia mosambica)

Phosphorylase from muscle of tilapia (Tilapia mosambica) was extracted by water and purified by ammonium sulphate precipitation, centrifugation and repeated recrystallisation. Electro-phorogram of the enzyme preparation showed a single band near origin. The enzyme showed optimum pH and temperature at 6.1 and 37°C respectively. Glucose and glucose-6-phosphate were found to be competitive inhibitors of the enzyme. Maltose and starch acted as primers for the phosphorylase reaction like glycogen.

Relationship between water, lipid and protein in the muscle, liver and gonad in a freshwater fish Puntius filamentosus (Val.)

Details are given of a study investigating the relationship between water, lipid, and protein in Puntius filamentosus. Percentage compositions in the muscle, liver and gonad of fish specimens from Lake Vellayani in India are given, showing the fluctuations which occur during maturation.