Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting.
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| Title: | Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting. |
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| Authors: | Nogueira, Laísa Santana1 (AUTHOR), Tavares, Iasnaia Maria de Carvalho1 (AUTHOR), Santana, Nívio Batista1 (AUTHOR), Ferrão, Sibelli Passini Barbosa1 (AUTHOR), Teixeira, Jabson Meneses2 (AUTHOR), Costa, Floriatan Santos3 (AUTHOR), Silva, Tatielle Pereira4 (AUTHOR), Pereira, Hugo Juarez Vieira4 (AUTHOR), Irfan, Muhammad5 (AUTHOR), Bilal, Muhammad6 (AUTHOR), de Oliveira, Julieta Rangel7 (AUTHOR), Franco, Marcelo7 (AUTHOR) marcelofranco@globo.com |
| Source: | Biotechnology & Applied Biochemistry. Oct2022, Vol. 69 Issue 5, p2069-2080. 12p. |
| Subjects: | Trypsin, Solid-state fermentation, Cocoa, Penicillium, Blood coagulation, Proteolytic enzymes, Milk, Fermentation |
| Abstract: | 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] |
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| Database: | Engineering Source |
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| Abstract: | 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] |
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| ISSN: | 08854513 |
| DOI: | 10.1002/bab.2268 |
