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Artigo Acesso aberto Produção Nacional Revisado por pares

BIBTEX RIS

Biotechnological potential of a cysteine protease (CpCP3) from Calotropis procera latex for cheesemaking

2019; Elsevier BV; Volume: 307; Linguagem: Inglês

10.1016/j.foodchem.2019.125574

1873-7072

Maria Z.R. Silva, João Paulo Bestete de Oliveira, Márcio V. Ramos, Davi Felipe Farias, Chayenne Alves de Sá, Juliana A.C. Ribeiro, Ayrles F.B. Silva, J. S. de Sousa, Rafael Audino Zambelli, Ana C. da Silva, Gilvan Pessoa Furtado, Thalles B. Grangeiro, Mirele S. Vasconcelos, Sandro Rios Silveira, Cléverson D.T. Freitas,

Vitamin K Research Studies

This article reports the characterization and evaluation of the biotechnological potential of a cysteine protease purified from Calotropis procera (CpCP3). This enzyme was highly stable to different metal ions and was able to hydrolyze κ-casein similarly to bovine chymosin. Atomic force microscopy showed that the process of casein micelle aggregation induced by CpCP3 was similar to that caused by chymosin. The cheeses made using CpCP3 showed higher moisture content than those made with chymosin, but protein, fat, and ash were similar. The sensory analysis showed that cheeses made with CpCP3 had high acceptance index (>80%). In silico analysis predicted the presence of only two short allergenic peptides on the surface of CpCP3, which was highly susceptible to digestive enzymes and did not alter zebrafish embryos' morphology and development. Moreover, recombinant CpCP3 was expressed in Escherichia coli. All results support the biotechnological potential of CpCP3 as an alternative enzyme to chymosin.