Characteristics of Collagen from Rohu (Labeo rohita) Skin

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from rohu skin with the yield of 64.2 and 6.8% (dry weight basis), respectively. Both collagens had glycine as the major amino acid with imino acid content of 196–202 residues/1,000 residues and were characterized as type I collagen with molecular composition of (α1)₂α2-heterotrimer. Fourier transform infrared spectra of both collagens were similar, with no shift in wavenumber of all amide bands. The T_max value of ASC and PSC was 36.40 and 35.48°C, respectively. The zero surface net charge of ASC and PSC was found at pH 5.9 and 5.3, respectively.     

Inhibitory effect of mimosine on polyphenoloxidase from cephalothoraxes of Pacific white shrimp (Litopenaeus vannamei)

The inhibitory effect of mimosine on polyphenoloxidase (PPO) from the cephalothorax of Pacific white shrimp (Litopenaeus vannamei) was studied. Mimosine showed inhibitory activity toward PPO from white shrimp with an apparent molecular weight of 210 kDa as evidenced by the decrease in the activity staining band, as compared to the control. An inhibition kinetic study revealed that mimosine exhibited the mixed type reversible inhibition on PPO from white shrimp with a Ki value of 3.7 mM. Mimosine showed copper (Cu2+) reduction and chelating capacity in a dose dependent manner. Mimosine could react with the intermediate browning product, thereby rendering lower red-brown color formation. Therefore, mimosine could inhibit PPO by different modes of inhibition and could be used to prevent melanosis formation in Pacific white shrimp.     

Quality Indices of Squid (Photololigo duvaucelii) and Cuttlefish (Sepia aculeata) Stored in Ice

The objective quality indices of squid (Photololigo duvaucelii) and cuttlefish (Sepia aculeata) stored in ice were compared with the subjective counterparts. Sensory (overall quality rating, quality index method [QIM], and multisample difference test), microbiological (total viable count [TVC], psychrophilic count), chemical (trichloroacetic acid-soluble peptide [TCA-soluble peptide], trimethylamine nitrogen [TMA-N], total volatile bases nitrogen [TVB-N], ammonia content, and protein pattern), and physical analyses (expressible drip, color, and texture) were determined in both species during 16 days of iced storage. As storage time increased, TCA-soluble peptide, TVB, ammonia content, and expressible drip were increased (p < 0.05). TMA content was markedly increased after 10 and 8 days of storage in squid and cuttlefish, respectively. Both TVC and psychrophilic count increased as the storage time increased (p < 0.01). Myosin heavy chain was degraded with coincidental decrease in shear force and sensory texture during storage (p < 0.05). According to the overall rating score, shelf life of both species in ice was estimated to be 6 days. The increases in ammonia content and expressible drip were highly correlated with the decrease in overall quality rating and increase in quality index score of squid and cuttlefish (p < 0.01).     

Chemical composition and physical properties of salted shrimp paste (Kapi) produced in Thailand

Chemical composition and physical properties of 11 salted shrimp pastes (Kapi) obtained from various places of Thailand were determined. Based on proximate composition, protein constituted the major component (29.44–53.27 %, dry wt. basis). All samples contained 22.77–35.47 % NaCl with A _w of 0.695–0.774. Various formal nitrogen contents (11.96–22.87 mg N/g sample) were in agreement with different degrees of hydrolysis (12.68–20.76 %), suggesting the varying cleavage of peptides among the samples. From electrophoretic study, salted shrimp paste contained a large amount of small molecular weight proteins and peptides. Different samples had different colors with \( \Delta E^{*} \) of 47.10–60.43 and \( \Delta C^{*} \) of 9.46–20.76. The samples had total carotenoid content of 0.54–1.97 mg/g sample. Free astaxanthin, astaxanthin diester and canthaxanthin were the major carotenoids in salted shrimp paste. Thus, salted shrimp paste is a good source of protein and serves as the nutritious condiment.     

Astaxanthin degradation and lipid oxidation of Pacific white shrimp oil: kinetics study and stability as affected by storage conditions

The kinetics of astaxanthin degradation and lipid oxidation in shrimp oil from hepatopancreas of Pacific white shrimp (Litopenaeus vannamei) as affected by storage temperature were studied. When shrimp oil was incubated at different temperatures (4, 30, 45 and 60 °C) for 16 h, the rate constants (k) of astaxanthin degradation and lipid oxidation in shrimp oil increased with increasing temperatures (p < 0.05). Thus, astaxanthin degradation and lipid oxidation in shrimp oil were augmented at high temperature. When shrimp oils with different storage conditions (illumination, oxygen availability and temperature) were stored for up to 40 days, astaxanthin contents in all samples decreased throughout storage (p < 0.05). All factors were able to enhance astaxanthin degradation during 40 days of storage. With increasing storage time, the progressive formation of primary and secondary oxidation products were found in all samples as evidenced by the increases in both peroxide values (PV) and thiobarbituric acid reactive substances (TBARS) (p < 0.05). Light, air and temperatures therefore had the marked effect on astaxanthin degradation and lipid oxidation in shrimp oils during the extended storage.     

Purification and characterization of trypsin from the spleen of tongol tuna (Thunnus tonggol)

Trypsin from tongol tuna (Thunnus tonggol) spleen was purified to 402-fold by ammonium sulfate precipitation, followed by a series of chromatographic separations. The molecular mass of trypsin was estimated to be 24 kDa by size-exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Trypsin appearing as a single band on native PAGE showed the maximal activity at pH 8.5 and 65 degrees C. It was stable in a wide pH range of 6-11 but unstable at the temperatures greater than 50 degrees C. The enzyme required calcium ion for thermal stability. The activity was strongly inhibited by 1.0 g/L soybean trypsin inhibitor and 5 mM TLCK and partially inhibited by 2 mM ethylenediaminetetraacetic acid. Activity was lowered with an increasing NaCl concentration (0-30%). The enzyme had a Km for Nalpha-p-tosyl-L-arginine methyl ester hydrochloride of 0.25 mM and a Kcat of 200 s-1. The N-terminal amino acid sequence of trypsin was determined as IVGGYECQAHSQPHQVSLNA and was very homologous to other trypsins.     

Antioxidant and Angiotensin-Converting Enzyme Inhibitory Activities of Protein Hydrolysates Prepared from Threadfin Bream (Nemipterus spp.) Surimi By-products

Solid wastes from threadfin bream (Nemipterus spp.) surimi production composed of head and frame were hydrolyzed by various commercial proteases (Alcalase, Flavourzyme, Neutrase, Protamex, papain, and pepsin) to produce protein hydrolysates with bioactive properties. An Alcalase-hydrolyzed sample at 24.4% degree of hydrolysis (DH) displayed the highest antioxidant activity based on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging, ferric reducing antioxidant power (FRAP) assay, and potassium ferricyanide method. In addition, it showed an inhibitory activity toward angiotensin-converting enzyme (ACE) of 25.5%. Antioxidant activity of threadfin bream by-product hydrolysates increased with hydrolysis time and reached the highest DPPH activity after 6 h, while that hydrolyzed for 3 h showed the highest reducing power based on FRAP and potassium ferricyanide assays. In addition, ACE inhibitory activity was found to be at an optimum after 3 h of hydrolysis. The hydrolysates (1 mg/mL) also retarded oxidation of a linoleic acid emulsion system to a similar extent as 0.1 mg/mL 3-tert-butyl-4-hydroxy anisole (BHA), indicating a potential use in the food system. Protein hydrolysates from threadfin bream surimi by-products could be tailor-made to possess both antioxidant and ACE inhibitory activity through controlling DH of Alcalase-catalyzed reactions.     

29 kDa Trypsin from the pyloric ceca of Atlantic Bonito (Sarda sarda): recovery and characterization

Trypsin from the pyloric ceca of Atlantic bonito (Sarda sarda) was purified and characterized with respect to its purity; molecular weight; sensitivity to temperature, pH, and inhibition; and N-terminal sequence. The purified trypsin had a molecular weight of 29 kDa as per sodium dodecyl sulfate polyacrylamide gel electrophoresis, and optimal activity was observed at pH 9 and 65 degrees C with BAPNA as a substrate. The enzyme was stable to heat treatment up to 50 degrees C and within the pH range of 7-12. It was stabilized by calcium ions, but its activity was strongly inhibited by soybean trypsin inhibitor, N-p-tosyl-L-lysine chloromethyl ketone, and phenyl methyl sulfonyl fluoride. The enzyme exhibited a progressive decrease in activity with increasing NaCl concentration (0-30%). The N-terminal 20 amino acid residues of Atlantic bonito trypsin were determined as IVGGYECQAHSQPWQPVLNS and were homologous with other trypsins.     

Quality changes of shrimp cracker covered with fish gelatin film without and with palm oil incorporated during storage

Impact of fish gelatin film incorporated without and with palm oil on the quality changes of fried shrimp cracker stored for 15 days at room temperature was investigated, in comparison with nylon/linear low-density polyethylene (nylon/LLDPE) film. The moisture content and water activity of shrimp cracker packaged with all films increased during storage (p < 0.05). The lowest moisture content and water activity were found in the sample packaged with nylon/LLDPE film throughout the storage (p < 0.05). Sample packaged with fish gelatin films incorporated with palm oil generally had lower moisture content than those without oil added during the first 12 days of storage (p < 0.05). During 15 days of storage, shrimp cracker packaged with nylon/LLDPE film generally had the lower PV and TBARS value as well as volatile compounds, except for n-nonanal, than those stored in fish gelatin films, regardless of oil incorporation. The decrease in crispiness and increase in toughness occurred in all samples during the 15 days of storage. Nevertheless, the lower changes were observed in the sample packaged with nylon/LLDPE film. Overall, gelatin film showed excellent oxygen barrier property, which was associated with the retardation of lipid oxidation. The incorporation of oil into gelatin film could lower WVP, but negatively increased oxygen permeability of the resulting film. Thus, the improvement of gelatin film is still required.