| Autor: |
Nogueira, Laísa Santana, Tavares, Iasnaia Maria de Carvalho, Santana, Nívio Batista, Ferrão, Sibelli Passini Barbosa, Teixeira, Jabson Meneses, Costa, Floriatan Santos, Silva, Tatielle Pereira, Pereira, Hugo Juarez Vieira, Irfan, Muhammad, Bilal, Muhammad, de Oliveira, Julieta Rangel, Franco, Marcelo |
| Předmět: |
|
| Zdroj: |
Biotechnology & Applied Biochemistry; Oct2022, Vol. 69 Issue 5, p2069-2080, 12p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Plný text