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A study of metabolic rates of Poecilia reticulata Peters under different conditions (1993)

TEO, LENG-HONG ; CHEN, TI-WEN

Oxford, UK : Blackwell Publishing Ltd

Aquaculture research 24 (1993), S. 0

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ISSN: 1365-2109

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition

Notes: Abstract. The aim of this work was to investigate the factors that affect the metabolic rates of guppies, Poecilia reticulata Peters, by measuring the oxygen uptakes of guppies individually or in groups in closed vessels to simulate the actual packaging condition. Metabolic rates of guppies increased with the increase of temperatures. Anaesthetic, 2-phenoxyethanoll suppressed the oxygen consumption rates. Grouped fish also showed lower metabolic rates than individual fish. Light and starvation did not produce any effect. The pH of the water, ammonium and carbon dioxide concentrations had significant effects on the metabolic rates of guppies.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2109.1993.tb00833.x

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Some properties of the intestinal proteases of the rabbitfish, Siganus canaliculatus (Park) (1995)

Sabapathy, Uma ; Teo, Leng-Hong

Springer

Fish physiology and biochemistry 14 (1995), S. 215-221

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ISSN: 1573-5168

Keywords: trypsin ; chymotrypsin ; leucine aminopeptidase ; proteases ; fish ; digestion

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Some properties of the intestinal proteases of the rabbitfish were examined. At 25°C, both trypsin and chymotrypsin showed pH optima of 8.0. Leucine aminopeptidase, however, displayed maximum activity in the pH range, 7.0–9.0. Leucine aminopeptidase had the highest optimum temperature (60°C), and chymotrypsin, the lowest (30°C). The optimum temperature of trypsin was 55°C. The activation energy, Ea, was found to be 8.24 for trypsin and 8.50 kcal mol−1 for chymotrypsin. The Ea for leucine aminopeptidase was 6.29 kcal mol−1 above 40°C and 1.73 kcal mol−1 below 40°C. Substrate concentration-velocity plots showed that all three enzymes followed Michaelis-Menten kinetics; the Km and Vmax were estimated for the three enzymes. The effects of various protease inhibitors on enzyme activity were also examined and confirmed the protease classes to which each enzyme belonged. The three proteases examined have similar properties to proteases in other fishes.