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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.
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]
Copyright of Biotechnology & Applied Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting.
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  Data: <searchLink fieldCode="AR" term="%22Nogueira%2C+Laísa+Santana%22">Nogueira, Laísa Santana</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Tavares%2C+Iasnaia+Maria+de+Carvalho%22">Tavares, Iasnaia Maria de Carvalho</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Santana%2C+Nívio+Batista%22">Santana, Nívio Batista</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ferrão%2C+Sibelli+Passini+Barbosa%22">Ferrão, Sibelli Passini Barbosa</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Teixeira%2C+Jabson+Meneses%22">Teixeira, Jabson Meneses</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Costa%2C+Floriatan+Santos%22">Costa, Floriatan Santos</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Silva%2C+Tatielle+Pereira%22">Silva, Tatielle Pereira</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Pereira%2C+Hugo+Juarez+Vieira%22">Pereira, Hugo Juarez Vieira</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Irfan%2C+Muhammad%22">Irfan, Muhammad</searchLink><relatesTo>5</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bilal%2C+Muhammad%22">Bilal, Muhammad</searchLink><relatesTo>6</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22de+Oliveira%2C+Julieta+Rangel%22">de Oliveira, Julieta Rangel</searchLink><relatesTo>7</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Franco%2C+Marcelo%22">Franco, Marcelo</searchLink><relatesTo>7</relatesTo> (AUTHOR)<i> marcelofranco@globo.com</i>
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  Data: <searchLink fieldCode="JN" term="%22Biotechnology+%26+Applied+Biochemistry%22">Biotechnology & Applied Biochemistry</searchLink>. Oct2022, Vol. 69 Issue 5, p2069-2080. 12p.
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  Data: <searchLink fieldCode="DE" term="%22Trypsin%22">Trypsin</searchLink><br /><searchLink fieldCode="DE" term="%22Solid-state+fermentation%22">Solid-state fermentation</searchLink><br /><searchLink fieldCode="DE" term="%22Cocoa%22">Cocoa</searchLink><br /><searchLink fieldCode="DE" term="%22Penicillium%22">Penicillium</searchLink><br /><searchLink fieldCode="DE" term="%22Blood+coagulation%22">Blood coagulation</searchLink><br /><searchLink fieldCode="DE" term="%22Proteolytic+enzymes%22">Proteolytic enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Milk%22">Milk</searchLink><br /><searchLink fieldCode="DE" term="%22Fermentation%22">Fermentation</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: 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]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Biotechnology & Applied Biochemistry is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1002/bab.2268
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 12
        StartPage: 2069
    Subjects:
      – SubjectFull: Trypsin
        Type: general
      – SubjectFull: Solid-state fermentation
        Type: general
      – SubjectFull: Cocoa
        Type: general
      – SubjectFull: Penicillium
        Type: general
      – SubjectFull: Blood coagulation
        Type: general
      – SubjectFull: Proteolytic enzymes
        Type: general
      – SubjectFull: Milk
        Type: general
      – SubjectFull: Fermentation
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      – TitleFull: Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting.
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              M: 10
              Text: Oct2022
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              Y: 2022
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