EXTRAÇÃO DE ENZIMA COLAGENOLÍTICA DAS VÍSCERAS DE PEIXES POR PARTIÇÃO DE FASES (PEG/CITRATO) E SEU POTENCIAL PARA APLICAÇÃO INDUSTRIAL
DOI:
https://doi.org/10.20950/1678-2305.2020.46.4.593Palavras-chave:
Biotechnology;, collagenase;, by-products;, residue.Resumo
Vísceras internas de peixes são fontes potenciais de biomoléculas proteicas de interesse biofarmacêutico. No entanto, esse resíduo é frequentemente descartado de forma inadequada. A possibilidade de obtenção de subprodutos de maior valor agregado é uma realidade. Dentro desta visão, atenção deve ser dada aos processos de recuperação e extração de moléculas-alvo. Como o alto custo do processamento desses resíduos é um dos obstáculos para sua reutilização, técnicas que facilitem seu manuseio e barateiem o processo são desejáveis, como a extração em sistema bifásico. Assim, o objetivo deste estudo foi extrair enzimas colagenolíticas de robaloflecha (Centropomus undecimalis) usando sistema bifásico (polietilenoglicol/citrato), de acordo com o planejamento fatorial 24, tendo como variáveis: massa molar do PEG (MPEG), concentração de PEG (CPEG), concentração de citrato (CCIT), e pH; ainda, considerando: fator de purificação (PF), coeficiente de partição (K) e rendimento (Y) como respostas. A atividade colagenolítica do
extrato bruto foi de 102,41 U mg-1. Após o particionamento, a amostra foi purificada 3,91 vezes (MPEG: 8000; CPEG: 20,0%; CCIT: 20,0% e pH 6,0), sendo inibida (U mg-1) pela benzamidina (22,51), TLCK (21,05), TPCK (21,29), e PMSF (23,08), sinalizando tratar-se de uma serino-protease. Os resultados mostraram a vantagem desta técnica de semipurificação no que diz respeito ao baixo custo de extração e purificação, valorizando a matéria-prima pesqueira e destinando os resíduos de seu processamento para a indústria.
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Barros Neto, B.; Scarminio, I.S.; Bruns, R.E. 2003. Como fazer experimentos: pesquisa e desenvolvimento na ciência e na indústria. 2ª. ed. Campinas: Unicamp. 401p.
Bhagwat, P.; Dandge, P. 2018. Collagen and collagenolytic proteases: A review. Biocatalysis and Agricultural Biotechnology, 15: 43-55. http://dx.doi.org/10.1016/j.bcab.2018.05.005.
Chen-Roetling, J.; Cao, Y.; Peng, D.; Regan, R.F. 2019. Rapid loss of perihematomal cell viability in the collagenase intracerebral hemorrhage model. Brain Research, 1711: 91-96. http://dx.doi.org/10.1016/j.brainres.2019.01.014.
Concha-Frias, B.B.; Alvarez-González, C.A.; Gaxiola-Cortes, M.G.; Silva-Arancibia, A.E.; Toledo-Agüero, P.H.; Martínez-García, R.; Camarillo-Coop, S.; Jimenez-Martinez, L.D.; Arias-Moscoso, J.L. 2016. Partial characterization of digestive proteases in the Common snook Centropomus undecimalis. International Journal of Biology, 8(4): 1-11. http://dx.doi.org/10.5539/ijb.v8n4p1.
Gurumallesh, P.; Alagu, K.; Ramakrishnan, B.; Muthusamy, S. 2019. A systematic reconsideration on proteases. International Journal of Biological Macromolecules, 128: 254-256. http://doi.org/10.1016/j.ijbiomac.2019.01.081.
Ideia, P.; Pinto, J.; Ferreira, R.; Figueiredo, L.; Spínola, V.; Castilho, P.C. 2020. fish processing industry residues: a review of valuable products extraction and characterization methods. Waste and Biomass Valorization, 11: 3223-3246. http://dx.doi.org/10.1007/s12649-019-00739-1.
Iqbal, M.; Tao, Y.; Xie, S.; Zhu, Y.; Chen, D.; Wang, X.; Huang, L.; Peng, D.; Sattar, A.; Shabbir, M.A.B.; Hussain, H.I.; Ahmed, S.; Yuan, Z. 2016. Aqueous two-phase system (ATPS): An overview and advances in its applications. Biological Procedures Online, 18: 1-18. http://dx.doi.org/10.1186/s12575-016-0048-8.
Jimenez-Martinez, L.D.; Alvarez-González, C.A.; Tovar-Ramírez, D.; Gaxiola, G.; Sanchez-Zamora, A.; Moyano, F.J.; Alarcón, F.J.; Marquez-Couturier, G.; Gisbert, E.; Contreras-Sánchez, W.M.; Perales-Garcia, N.; Arias-Rodrıguez, L.; Indy, J.R.; Páramo-Delgadillo, S.; Palomino-Albarran, I.G. 2012. Digestive enzyme activities during early ontogeny in Common snook (Centropomus undecimalis). Fish Physiology and Biochemistry, 38(2): 441-454. http://dx.doi.org/10.1007/s10695-011-9525-9.
Ketnawa, S.; Benjakul, S.; Ling, T.C.; Martínez-Alvarez, O.; Rawdkuen, S. 2013. Enhanced recovery of alkaline protease from fish viscera by phase partitioning and its application. Chemistry Central Journal, 7: 1-9. http://dx.doi.org/10.1186/1752-153X-7-79.
Kuepethkaew, S.; Sangkharak, K.; Benjakul, S.; Klomklao, S. 2017. Use of TPP and ATPS for partitioning and recovery of lipase from Pacific white shrimp (Litopenaeus vannamei) hepatopancreas. Journal of Food Science and Technology, 54: 3880-3891. http://dx.doi.org/10.1007/s13197-017-2844-9.
Kim, S.K.; Park, P.J.; Kim, J.B.; Shahidi, F. 2002. Purification and characterization of a collagenolytic protease from the filefish, Novoden modestrus. Journal of Biochemistry and Molecular Biology, 35(2): 165-171. http://dx.doi.org/10.5483/bmbrep.2002.35.2.165.
Leong, Y.K.; Lan, J.C.-W.; Loh, H.-S.; Ling, T.C.; Ooi, C.W.; Show, P.L. 2015. Thermoseparating aqueous two-phase systems: Recent trends and mechanisms. Journal of Separation Science, 39(4): 640-647. http://dx.doi.org/10.1002/jssc.201500667.
Liu, Y.; Liu, Z.; Song, L.; Ma, Q.; Zhou, D.; Zhu, B.; Shahidi, F. 2019. Effects of collagenase type I on the structural features of collagen fibres from sea cucumber (Stichopus japonicus) body wall. Food Chemistry, 301: 1-7. http://dx.doi.org/10.1016/j.foodchem.2019.125302.
Nadar, S.S.; Pawar, R.G.; Rathod, V.K. 2017. Recent advances in enzyme extraction strategies: A comprehensive review. International Journal of Biological Macromolecules, 101: 931-957. http://dx.doi.org/10.1016/j.ijbiomac.2017.03.055.
Oliveira, V.M.; Assis, C.R.D.; Herculano, P.N.; Cavalcanti, M.T.H.; Bezerra, R.S.; Porto, A.L.F. 2017a. Collagenase from smooth weakfish: extraction, partial purification, characterization and collagen specificity test for industrial application. Boletim do Instituto de Pesca, 43(1): 52-64. http://dx.doi.org/10.20950/1678-2305.2017v43n1p52.
Oliveira, V.M.; Nascimento, T.P.; Assis, C.R.D.; Bezerra, R.S.; Porto, A.L.F. 2017b. Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili). Journal of Coastal Life Medicine, 5(6): 233-238. http://dx.doi.org/10.12980/jclm.5.2017J6-300.
Oliveira, V.M.; Carneiro Cunha, M.N.; Assis, C.R.D.; Nascimento, T.P.; Herculano, P.N.; Cavalcanti, M.T.H.; Porto, A.L. 2017c. Colagenases de pescado e suas aplicações industriais. Pubvet, 11(3): 243-255. http://dx.doi.org/10.22256/PUBVET.V11N3.243-255.
Oliveira, V.M.; Assis, C.R.D.; Silva, J.C.; Silva, Q.J.; Bezerra, R.S.; Porto, A.L.F. 2019. Recovery of fibrinolytic and collagenolytic enzymes from fish and shrimp byproducts: potential source for biomedical applications. Boletim do Instituto de Pesca, 45(1): 1-10. http://dx.doi.org/10.20950/1678-2305.2019.45.1.389.
Oliveira, V.M.; Cunha, M.N.C.; Assis, C.R.D.; Silva, J.M.; Nascimento, T.P.; Santos, J.F.; Duarte, C.A.L.; Marques, D.A.V.; Bezerra, R.S.; Porto, A.L.F. 2020. Separation and partial purification of collagenolytic protease from peacock bass (Cichla ocellaris) using different protocol: Precipitation and partitioning approaches. Biocatalysis and Agricultural Biotechnology, 24: 1-13. http://dx.doi.org/10.1016/j.bcab.2020.101509.
Park, J.P.; Lee, S.H.; Byun, H.G.; Kim, S.H.; Kim, S.K. 2002. Purification and characterization of a collagenase from the mackerel, Scomber japonicus. Journal of Biochemistry and Molecular Biology, 35(6): 576-582. http://dx.doi.org/10.5483/bmbrep.2002.35.6.576.
Phong, W.N.; Show, P.L.; Chow, Y.H.; Ling, T.C. 2018. Recovery of biotechnological products using aqueous two-phase systems. Journal of Bioscience and Bioengineering, 126(3): 273-281. http://dx.doi.org/10.1016/j.jbiosc.2018.03.005.
Poonsin, T.; Sripokar, P.; Benjakul, S.; Simpson, B.K.; Visessanguan, W.; Klomklao, S. 2017. Major trypsin like-serine proteinases from albacore tuna (Thunnus alalunga) spleen: biochemical characterization and the efect of extraction media. Journal of Food Biochemistry, 41(2): 1-9. http://dx.doi.org/10.1111/jfbc.12323.
Porto, T.S.; Pessôa-Filho, P.A.; Neto, B.B.; Filho, J.L.L.; Converti, A.; Porto, A.L.F.; Pessoa, A. 2007. Removal of proteases from Clostridium perfringens fermented broth by aqueous two-phase systems (PEG/citrate). Journal of Industrial Microbiology & Biotechnology, 34(8): 547-552. http://dx.doi.org/10.1007/s10295-007-0230-8.
Rosso, B.U.; Lima, C.D.A.; Porto, T.S.; Nascimento, C.O.; Pessoa, A.; Converti, A.; Carneiro-da-Cunha, M.D.G.; Porto, A.L.F. 2012. Partitioning and extraction of collagenase from Penicillium aurantiogriseum in poly(ethylene glycol)/phosphate aqueous two-phase system. Fluid Phase Equilibria, 335: 20-25. http://dx.doi.org/10.1016/j.fluid.2012.05.030.
Roy, P.; Bernard, C.; Patrick, D. 1996. Purification, kinetical and molecular characterizations of a serine collagenolytic protease from green shore Crab (Carcinus maenas) digestive gland. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 115(1): 87-95. http://dx.doi.org/10.1016/0305-0491(96)00090-9.
Senphan, T.; Benjakul, S. 2014. Antioxidative activities of hydrolysates from seabass skin prepared using protease from hepatopancreas of Pacific white shrimp. Journal of Functional Foods, 6: 147-156. http://dx.doi.org/10.1016/j.jff.2013.10.001.
Silva, J.C.; Silva, Q.G.; Oliveira, V.M.; Porto, A.L.F. 2019. Uso de resíduos orgí¢nicos de anchova (Pomatomus saltatrix) e robalo-flecha (Centropomus undecimalis) para recuperação de proteases alcalinas. In: Aguiar, A.C.;
Silva, K.A.; Giovanettiel-Deir, S. (orgs). Resíduos sólidos: impactos ambientais e inovações tecnológicas. 1ª ed. Recife: EDUFRPE, p. 117-126.
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2021-03-27
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