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ABSTRACT

Postmortem biochemical and microbiological changes in loricariid catfish (Pterygoplichthys disjunctivus) muscle were evaluated during ice storage for 20 days. Values of pH remained stable for 15 days (7.4 ± 0.2), and total volatile base-nitrogen (TVB-N) remained under acceptable limits throughout storage, with a final value of 25.2 ± 3.3 mg N/100 g muscle at Day 20. Adenosine-5´-triphosphate (ATP) and derivatives followed a postmortem degradation pattern similar to other species, with the K-value being the best freshness loss indicator. Biochemical and microbiological changes indicated that the shelf life of iced loricariid catfish muscle was 15 days under optimal (0°C) storage conditions.  相似文献   
2.
Vermiculated sailfin catfish (Pterygoplichthys disjunctivus, Weber, 1991), a member of the Loricariidae family and an invasive species of several inland waters around the world, possess an enormous digestive tract representing about 10% of fish weight. Thus, the aim of this study was to partially characterize proteases from their digestive tracts. Azocasein digestion of the crude extract of intestine at different pH values and temperatures revealed the presence of alkaline proteases with optimum activities at pH 9.0 and 50°C. Incubation assays of the crude extract with inhibitors such as phenyl methyl sulfonyl fluoride, N-α-p-tosyl-l-lysine chloromethyl ketone, N-tosyl-phenyalanine chloromethyl ketone, benzamidine, pepstatin A and ethylenediamine tetra-acetic acid showed that trypsin and chymotrypsin are the main alkaline proteinases present. Zymography showed that the crude extract of Pterygoplichthys disjunctivus viscera contained proteases with molecular masses ranging from 21.5 to 116 kDa. Trypsin and chymotrypsin were inhibited by the following ions in decreasing order: Hg2+, Fe2+, Cu2+, Li+, Mg2+, K+, while Mn2+, and Ca2+ had no effect. Activities decreased continuously as the NaCl concentration increased from 0 to 30%. These results constitute important background information for future studies and for the potential biotechnological use of the crude digestive extract from this invasive species.  相似文献   
3.
Pterygoplichthys disjunctivus viscera chymotrypsin was purified by fractionation with ammonium sulfate (30–70 % saturation), gel filtration, affinity, and ion exchange chromatography. Chymotrypsin molecular weight was approximately 29 kDa according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), shown a single band in zymogram. Electrofocusing study suggested being an anionic enzyme (pI ≈ 3.9), exhibiting maximal activity at pH 9 and 50 °C, using Suc-Ala-Ala-Pro-Phe-p-nitroanilide (SAAPNA) as substrate. Enzyme was effectively inhibited by phenyl methyl sulfonyl fluoride (PMSF) (99 %), and N-tosyl-l-phenylalanine chloromethyl ketone (TPCK) (94 %). Enzyme activity was affected by the following ions in decreasing order: Hg2+, Fe2+, Cu2+, Li1+, Mg2+, K1+, Mn2+, while Ca2+ had no effect. Chymotrypsin activity decreased continuously as NaCl concentration increased (from 0 to 30 %). K m and V max values were 0.72 ± 1.4 mM and 1.15 ± 0.06 μmol/min/mg of protein, respectively (SAAPNA as substrate). Results suggest the enzyme has a potential application where low processing temperatures are needed, such as in fish sauce production.  相似文献   
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