Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting

Autor: Julieta Rangel de Oliveira, Laísa Santana Nogueira, Floriatan Santos Costa, Nivio Batista Santana, Tatielle Pereira Silva, Iasnaia Maria de Carvalho Tavares, Hugo Juarez Vieira Pereira, Muhammad Irfan, Jabson Meneses Teixeira, Sibelli Passini Barbosa Ferrão, Marcelo Franco, Muhammad Bilal
Rok vydání: 2021
Předmět:
Zdroj: Biotechnology and Applied Biochemistry. 69:2069-2080
ISSN: 1470-8744
0885-4513
Popis: The increased demand for cheese and the limited availability of calf rennet justifies the search for milk-clotting enzymes from alternative sources. Trypsin-like protease by Penicillium roqueforti was produced by solid-state fermentation using cocoa shell waste as substrate. The production of a crude enzyme extract that is rich in this enzyme was optimized using a Doehlert-type multivariate experimental design. The biochemical characterization showed that the enzyme has excellent activity and stability at alkaline pH (10-12) and an optimum temperature of 80°C, being stable at temperatures above 60°C. Enzymatic activity was maximized in the presence of Na+ (192%), Co2+ (187%), methanol (153%), ethanol (141%), and hexane (128%). Considering the biochemical characteristics obtained and the milk coagulation activity, trypsin-like protease can be applied in the food industry, such as in milk clotting and in the fabrication of cheeses.
Databáze: OpenAIRE