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1.
Biol Trace Elem Res ; 201(1): 412-424, 2023 Jan.
Article in English | MEDLINE | ID: mdl-35201568

ABSTRACT

The effect of green tea (Camellia sinensis) iron oxide nanoparticles (nano-Fe) on the effectiveness, growth, antioxidant capacity, and immunological response of Trichogaster trichopterus (Blue gourami) fingerlings was investigated. UV-Visible, Fourier Transform Infrared, Scanning Electron Microscopy, Energy Dispersive X-ray, X-ray diffraction, Dynamic Light Scattering, and Zeta Potential spectroscopy were used to evaluate the biologically synthesized nano-Fe. Characterization revealed the hexagonal and spherical morphology with an average diameter of 114 nm. Six different experimental diets were supplied to the fish in duplicate for 60 days. The first diet served as a control (no nano-Fe supplementation), whereas the remaining five diets contained nano-Fe at concentrations of 10, 20, 30, 40, and 50 mg/kg (D1 to D5). The results indicated that fish fed a nano-Fe diet at a concentration of 40 mg/kg had improved growth performance, biochemical constituents, hematological parameters, and antioxidant activity in T. trichopterus, implying that it might be used as a vital feed supplement in ornamental fish culture.


Subject(s)
Antioxidants , Camellia sinensis , Animals , Antioxidants/pharmacology , Fishes , Dietary Supplements , Magnetic Iron Oxide Nanoparticles
2.
3 Biotech ; 6(2): 157, 2016 Dec.
Article in English | MEDLINE | ID: mdl-28330229

ABSTRACT

The quantum of marine fish wastes produced by fish processing industries has necessitated to search new methods for its disposal. Hence, this study is focused on production and purification of halophilic organic solvent tolerant protease (HOSP) from marine Alcaligenes faecalis APCMST-MKW6 using marine shell wastes as substrate. The candidate bacterium was isolated from the marine sediment of Manakudi coast and identified as A. faecalis APCMST-MKW6. The purified protease showed 16.39-fold purity, 70.34 U/mg specific activity with 21.67 % yield. The molecular weight of the purified alkaline protease was 49 kDa. This purified protease registered maximum activity at pH 9 and it was stable between pH 8-9 after 1.30 h of incubation. The optimum temperature registered was 60 °C and it was stable between 50 and 60 °C even after 1.30 h of incubation. This enzyme also showed maximum activity at 20 % NaCl concentration. Further, manganese chloride, magnesium chloride, calcium chloride and barium chloride influenced this enzyme activity remarkably and it was also found to be enhanced by many of the tested surfactants and solvents. The candidate bacterium effectively deproteinized the shrimp shell waste compared to the other tested crustaceans shell wastes and also attained maximum antioxidant activity.

3.
Biotechnol Rep (Amst) ; 8: 124-132, 2015 Dec.
Article in English | MEDLINE | ID: mdl-28352581

ABSTRACT

The current increase in the vast amount of marine crustacean shell waste produced by the fish processing industries has led to the need to find new methods for its disposal. Hence, the present study was carried out via marine shell wastes as substrate for protease production. The maximum production (4000.65 U/ml) from Bacillus sp. APCMST-RS3 was noticed in 3:1% shrimp and oyster shell powder (SOSP) as substrate. Purified protease showed 53.22% and 22.66% enzyme yield; 3.48 and 8.49 fold purity with 40 kDa molecular weight; whereas, its Km and Vmax values were 0.6666 g/l, 1111.11 U/ml. This enzyme showed optimum activity at pH 9 and 60 °C temperature. Also, it retained maximum protease activity in the presence of NaCl (2.5 M), surfactants (Tween 20, 40, 60, 80 and SDS) and metal ions (MnCl2, CaCl2, HgCl2 and BaCl2) and solvents. The candidate bacterium effectively deproteinized (84.35%) shrimp shell and its antioxidant potentials.

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