Abstract
Fish and shrimp industries generate a significant amount of by-products. These by-products can be used for the extraction of enzymes of biomedical interest, such as fibrinolytic and collagenolytic. Thus, this work aimed to perform a screening of fish and shrimp byproducts as sources of enzymes with fibrinolytic and collagenolytic activities and to characterize the biochemical properties of crude extracts with collagenolytic activity from Cichla ocellaris residues. Fibrinolytic enzymes were recovered with activities between 5.51 ± 0.02 U.mL-1 (Caranx crysos) and 56.16 ± 0.42 U.mL-1 (Litopenaeus vannamei), while collagenolytic enzymes were detected in a range between 6.79 ± 0.00 U.mg-1 (Trachurus lathami) and 94.35 ± 0.02 U.mg-1 (C. ocellaris). After collagenolytic screening, the selected species was C. ocellaris, being subjected to a preheating, which culminated with an increase of enzymatic activity of 35.07% (up to 127.44 ± 0.09 U.mg-1). The optimal collagenolytic activity recovered from C. ocellaris byproducts was 55 °C (thermostable between 25 and 60 °C) and 7.5 (stable between 6.5 and 11.5) for temperature and pH evaluations, respectively. The kinetic parameters were determined, obtaining Km of 5.92 mM and Vmax of 294.40 U.mg-1. The recovered enzyme was sensitive to the Cu2+, Hg2 and Pb2+ ions, being partially inhibited by phenylmethylsulphonyl fluoride (PMSF), N-p-tosyl-L-lysin chloromethyl ketone (TLCK) and Benzamidine. Furthermore, it was able to cleave native type I collagen, the most important type for industry. Thus, the recovery of biomolecules, besides offering to the industry an alternative source of active molecules, contributes to the reduction of the environmental impact, adding value to the fish product and providing a new source of income.
Highlights
World fish production has increased substantially to meet consumer demand
Fibrinolytic enzymes were recovered with activities between 5.51 ± 0.02 U.mL-1 (Caranx crysos) and 56.16 ± 0.42 U.mL-1 (Litopenaeus vannamei), while collagenolytic enzymes were detected in a range between 6.79 ± 0.00 U.mg-1 (Trachurus lathami) and 94.35 ± 0.02 U.mg-1 (C. ocellaris)
The fibrinolytic activity recovered from the byproducts of the species described in table 1 eminently suggest the potential of aquatic organisms as an alternative source of thrombolytic agents, corroborating with that described by Oliveira et al (2017d) when they recovered the fibrinolytic enzyme (26.70 ± 0.05 U.mL-1) of intestinal viscera of greater amberjack S. dumerili
Summary
World fish production has increased substantially to meet consumer demand. Thereby, the fish processing industries have generated significant quantities of organic material from daily processing waste (Daboor et al, 2010; Leite et al, 2016), with potential for industrial use after the accomplishment of bioprocesses of enzymatic recovery. For every 1 kg of fish, about 60 to 80% of this biomass is discarded by the fishing industry as devoid of commercial value, leading to environmental pollution from inadequate disposal. This discarded material includes head, tail, fins, scales and internal viscera, and of this latter, deserves attention the digestive ones because they are sources of several biomolecules of industrial interest such as proteins (Bezerra et al, 2006; Daboor et al, 2012; Freitas-Junior et al, 2012; Oliveira et al, 2017a). Fibrinolytic and collagenolytic enzymes gain special attention due to their physiological properties, the first to act as thrombolytic agents (Chandrashekar et al, 2018; Guedes et al, 2018), while the second to assist in healing processes (Alipour et al, 2017)
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