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

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 crud...

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Published in:	Biotechnology and applied biochemistry Vol. 69; no. 5; pp. 2069 - 2080
Main Authors:	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, Oliveira, Julieta Rangel, Franco, Marcelo
Format:	Journal Article
Language:	English
Published:	Calgary Wiley Subscription Services, Inc 01-10-2022
Subjects:	Biochemical characteristics biochemical characterization Biochemistry Carbon dioxide Cheese Clotting Coagulation Cobalt Cocoa Dairy products Design of experiments Doehlert design Enzymatic activity Ethanol Experimental design Fabrication Fermentation Food industry Fungi Hexanes Milk milk clotting Optimization Penicillium roqueforti Protease Proteinase Substrates Trypsin trypsin‐like protease
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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. The increased demand for cheese and the limited availability of calf rennet justifies the search for milk‐clotting enzymes from alternative sources.
AbstractList	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. The increased demand for cheese and the limited availability of calf rennet justifies the search for milk‐clotting enzymes from alternative sources. 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%), Co 2+ (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. 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.
Author	Ferrão, Sibelli Passini Barbosa Franco, Marcelo Tavares, Iasnaia Maria de Carvalho Nogueira, Laísa Santana Irfan, Muhammad Pereira, Hugo Juarez Vieira Bilal, Muhammad Costa, Floriatan Santos Silva, Tatielle Pereira Teixeira, Jabson Meneses Oliveira, Julieta Rangel Santana, Nívio Batista
Author_xml	– sequence: 1 givenname: Laísa Santana surname: Nogueira fullname: Nogueira, Laísa Santana organization: State University of Southwest Bahia – sequence: 2 givenname: Iasnaia Maria de Carvalho orcidid: 0000-0002-0478-7977 surname: Tavares fullname: Tavares, Iasnaia Maria de Carvalho organization: State University of Southwest Bahia – sequence: 3 givenname: Nívio Batista surname: Santana fullname: Santana, Nívio Batista organization: State University of Southwest Bahia – sequence: 4 givenname: Sibelli Passini Barbosa surname: Ferrão fullname: Ferrão, Sibelli Passini Barbosa organization: State University of Southwest Bahia – sequence: 5 givenname: Jabson Meneses surname: Teixeira fullname: Teixeira, Jabson Meneses organization: State University of Santa Cruz – sequence: 6 givenname: Floriatan Santos surname: Costa fullname: Costa, Floriatan Santos organization: Federal University of Paraná – sequence: 7 givenname: Tatielle Pereira surname: Silva fullname: Silva, Tatielle Pereira organization: Federal University of Alagoas – sequence: 8 givenname: Hugo Juarez Vieira orcidid: 0000-0003-2595-134X surname: Pereira fullname: Pereira, Hugo Juarez Vieira organization: Federal University of Alagoas – sequence: 9 givenname: Muhammad surname: Irfan fullname: Irfan, Muhammad organization: University of Sargodha – sequence: 10 givenname: Muhammad orcidid: 0000-0001-5388-3183 surname: Bilal fullname: Bilal, Muhammad organization: Huaiyin Institute of Technology – sequence: 11 givenname: Julieta Rangel surname: Oliveira fullname: Oliveira, Julieta Rangel organization: State University of Santa Cruz – sequence: 12 givenname: Marcelo orcidid: 0000-0002-7827-789X surname: Franco fullname: Franco, Marcelo email: marcelofranco@globo.com organization: State University of Santa Cruz
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Snippet	The increased demand for cheese and the limited availability of calf rennet justifies the search for milk‐clotting enzymes from alternative sources....
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SubjectTerms	Biochemical characteristics biochemical characterization Biochemistry Carbon dioxide Cheese Clotting Coagulation Cobalt Cocoa Dairy products Design of experiments Doehlert design Enzymatic activity Ethanol Experimental design Fabrication Fermentation Food industry Fungi Hexanes Milk milk clotting Optimization Penicillium roqueforti Protease Proteinase Substrates Trypsin trypsin‐like protease
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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