Abstract
BackgroundOver the past decades, the economic development and world population growth has led to increased for food demand. Increasing the fish production is considered one of the alternatives to meet the increased food demand, but the processing of fish leads to by-products such as skin, bones and viscera, a source of environmental contamination. Fish viscera have been reported as an important source of digestive proteases with interesting characteristics for biotechnological processes. Thus, the aim of this study was to purify and to characterize a trypsin from the processing by-products of crevalle jack (Caranx hippos) fish.ResultsA 27.5 kDa trypsin with N-terminal amino acid sequence IVGGFECTPHVFAYQ was easily purified from the pyloric caeca of the crevalle jack. Its physicochemical and kinetic properties were evaluated using N-α-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. In addition, the effects of various metal ions and specific protease inhibitors on trypsin activity were determined. Optimum pH and temperature were 8.0 and 50°C, respectively. After incubation at 50°C for 30 min the enzyme lost only 20% of its activity. K m , k cat, and k cat /K m values using BApNA as substrate were 0.689 mM, 6.9 s-1, and 10 s-1 mM-1, respectively. High inhibition of trypsin activity was observed after incubation with Cd2+, Al3+, Zn2+, Cu2+, Pb2+, and Hg2+ at 1 mM, revealing high sensitivity of the enzyme to metal ions.ConclusionsExtraction of a thermostable trypsin from by-products of the fishery industry confirms the potential of these materials as an alternative source of these biomolecules. Furthermore, the results suggest that this trypsin-like enzyme presents interesting biotechnological properties for industrial applications.
Highlights
IntroductionThe economic development and world population growth has led to increased for food demand
Over the past decades, the economic development and world population growth has led to increased for food demand
In the American continent, it is found from Nova Scotia to the Gulf of Mexico and Caribbean and as far south as the Uruguayan coastline [14]. This fish has significant commercial importance to the Brazilian fishery industry, with approximately 2,500 tons being captured along the Brazilian coast in 2010 [15]
Summary
The economic development and world population growth has led to increased for food demand. Fish processing generates large quantities of liquid and solid wastes including skin, bones, fins, heads, and viscera These by-products have no commercial value and are generally discarded without treatment, causing environmental pollution. Fishery by-products have been proposed as a low-cost source of biomolecules such as proteases [1,2,3,4,5,6] These digestive enzymes constitute one of Crevalle jack (Caranx hippos) is a marine fish found in tropical and subtropical zones worldwide. In the American continent, it is found from Nova Scotia to the Gulf of Mexico and Caribbean and as far south as the Uruguayan coastline [14] This fish has significant commercial importance to the Brazilian fishery industry, with approximately 2,500 tons being captured along the Brazilian coast in 2010 [15]. The objective of this study was to purify and partially characterize a thermostable trypsin from the pyloric caeca of C. hippos and determine its N-terminal sequence
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