Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

de Oliveira, Rodrigo Lira; de Souza Claudino, Emiliana; Converti, Attilio; Porto, Tatiana Souza

doi:10.3390/catal11080963

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Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

by

Rodrigo Lira de Oliveira

¹

,

Emiliana de Souza Claudino

¹,

Attilio Converti

^2,*

and

Tatiana Souza Porto

³

¹

School of Food Engineering, Federal University of Agreste of Pernambuco/UFAPE, Av. Bom Pastor, Boa Vista, s/n, Garanhuns 55296-901, Brazil

²

Department of Civil, Chemical and Environmental Engineering, Pole of Chemical Engineering, Genoa University, Via Opera Pia 15, 16145 Genoa, Italy

³

Department of Morphology and Animal Physiology, Federal Rural University of Pernambuco/UFRPE, Av. Dom Manoel de Medeiros, s/n, Recife 52171-900, Brazil

^*

Author to whom correspondence should be addressed.

Catalysts 2021, 11(8), 963; https://doi.org/10.3390/catal11080963

Submission received: 27 June 2021 / Revised: 8 August 2021 / Accepted: 10 August 2021 / Published: 11 August 2021

(This article belongs to the Special Issue Enzymes and Biocatalysis)

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Abstract

Microbial proteases are commonly produced by submerged (SmF) or solid-state fermentation (SSF), whose combination results in an unconventional method, called sequential fermentation (SF), which has already been used only to produce cellulolytic enzymes. In this context, the aim of the present study was the development of a novel SF method for protease production using wheat bran as a substrate. Moreover, the kinetic and thermodynamic parameters of azocasein hydrolysis were estimated, thus providing a greater understanding of the catalytic reaction. In SF, an approximately 9-fold increase in protease activity was observed compared to the conventional SmF method. Optimization of glucose concentration and medium volume by statistical means allowed us to achieve a maximum protease activity of 180.17 U mL⁻¹. The obtained enzyme had an optimum pH and temperature of 7.0 and 50 °C, respectively. Kinetic and thermodynamic parameters highlighted that such a neutral protease is satisfactorily thermostable at 50 °C, a temperature commonly used in many applications in the food industry. The results obtained suggested not only that SF could be a promising alternative to produce proteases, but also that it could be adapted to produce several other enzymes.

Keywords: Aspergillus; protease; sequential fermentation; kinetics; thermodynamics

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MDPI and ACS Style

de Oliveira, R.L.; de Souza Claudino, E.; Converti, A.; Porto, T.S. Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme. Catalysts 2021, 11, 963. https://doi.org/10.3390/catal11080963

AMA Style

de Oliveira RL, de Souza Claudino E, Converti A, Porto TS. Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme. Catalysts. 2021; 11(8):963. https://doi.org/10.3390/catal11080963

Chicago/Turabian Style

de Oliveira, Rodrigo Lira, Emiliana de Souza Claudino, Attilio Converti, and Tatiana Souza Porto. 2021. "Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme" Catalysts 11, no. 8: 963. https://doi.org/10.3390/catal11080963

APA Style

de Oliveira, R. L., de Souza Claudino, E., Converti, A., & Porto, T. S. (2021). Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme. Catalysts, 11(8), 963. https://doi.org/10.3390/catal11080963

Note that from the first issue of 2016, this journal uses article numbers instead of page numbers. See further details here.

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Use of a Sequential Fermentation Method for the Production of Aspergillus tamarii URM4634 Protease and a Kinetic/Thermodynamic Study of the Enzyme

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