Abstract
Resíduos do processamento do pescado são fontes ricas em biomoléculas com potencial industrial, como as enzimas com propriedades colagenolíticas empregadas nos segmentos farmacêuticos, têxteis e de couro. No presente trabalho, serino-proteases colagenolíticas dos resíduos (vísceras) do processamento de pescada-branca, Cynoscion leiarchus, foram parcialmente purificadas e caracterizadas, visando í obtenção de um produto de valor agregado, maximizando o aproveitamento de recursos pesqueiros. A atividade da melhor etapa de extração foi 72,5 U mL-1, com temperatura e pH ótimos de 55°C e 8,0 respectivamente. A enzima manteve-se estável em faixas amplas de temperatura (25í 60°C) e pH (6,5-11,5). Os íons Ca2+ e Mg2+ aumentaram a atividade proteolítica, ao passo que Pb2+, Al3+ e Cu2+ inibiram essa atividade, assim como os inibidores de serino-proteases (Benzamidina e TLCK). A hidrólise foi detectada após 48 h de incubação com colágeno bovino tipo I. Assim, sugere-se o emprego de vísceras digestivas de C. leiarchus como fonte alternativa de enzimas com capacidade de clivar o colágeno do tipo I e com propriedades bioquímicas semelhantes í s das colagenases bacterianas, já empregadas nas etapas de processamento industrial como forma de redução de custo e agregação de valor ao produto pesqueiro, contribuindo assim para minimizar o impacto ambiental deste tipo de resíduo.
Highlights
According to the Food and Agriculture Organization of the United Nations (FAO), in 2012, the global production of fish for human consumption was estimated to be approximately 136.2 million tons; which is responsible for providing 20% of animal protein to 2.9 billion people and expected to be increased to 151.77 million in 2030 (FAO, 2013; 2014)
The fraction with the highest collagenolytic activity was detected in step III, with an increase of 32% in relation to step I, as seen in Table 1, which shows the enzyme activity of the crude extract obtained from intestinal waste of smooth weakfish C. leiarchus
According to the results shown here, the crude extract of smooth weakfish C. leiarchus, after the successive stages of extraction, may be suggested as potential source of collagenolytic enzymes for application in several stages of leather processing due to their similar properties to commercial enzymes, operating as a non-toxic biocatalyst, improving dyeing characteristics and contributing to an ecologically viable process
Summary
According to the Food and Agriculture Organization of the United Nations (FAO), in 2012, the global production of fish for human consumption was estimated to be approximately 136.2 million tons; which is responsible for providing 20% of animal protein to 2.9 billion people and expected to be increased to 151.77 million in 2030 (FAO, 2013; 2014). Collagenases (EC 3.4.24.7) constitute a group of enzymes that hydrolyze the peptide bonds of various types of collagen, the most abundant protein in mammals, under physiological conditions of pH and temperature both in vivo and in vitro (DABOOR et al, 2010; HAYET et al, 2011; SOUCHET and LAPLANTE, 2011). They are highly specific for native or denatured collagen, showing no activity to any other protein. Collagenolytic enzymes are relevant for their biotechnological potential use in medicine, food industry, cosmetics, leather processing, and obtaining bioactive collagen peptides (DABOOR et al, 2010; KANTH et al, 2008; LIMA et al, 2013; SARAN et al, 2013)
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