Characterization and immobilization of protease secreted by the fungus Moorella speciosa
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ORIGINAL ARTICLE
Characterization and immobilization of protease secreted by the fungus Moorella speciosa Juliana Mota de Oliveira1 · Pedro Fernandes2,3 · Raquel Guimarães Benevides1 · Sandra Aparecida de Assis1 Received: 27 March 2020 / Accepted: 24 August 2020 © King Abdulaziz City for Science and Technology 2020
Abstract Protease was extracellularly produced in submerged fermentation by the fungus Moorella speciosa with maximum activity of 8.6 × 103 U/mL. The optimal pH and temperature for enzyme activity were 6.78 and 60.88 °C, respectively. The enzyme was incubated in the presence of several ions at concentrations of 0.1 M and 0.01 M to address the effect on enzyme activity. Enzyme activity was increased by 56% and 130% in the presence of 0.1 M BaCl2 and of 0.01 M Na2SO4, respectively. The Vmax and Km values were 0.01474 U/min/mg protein and 0.04190 mg/mL, respectively. The enzyme retained about 90% of enzymatic activity at 90 °C. Among the methods tested for enzyme immobilization, adsorption onto MAT540 carrier led to the most promising results, since after 15 reuse cycles up to 60% of the initial catalytic activity was retained. Entrapment in calcium alginate matrix allowed to retain up to 51% of the initial catalytic activity after 8 reuse cycles. This protease from M. speciosa, in either free or immobilized form, can be foreseen as a useful biocatalytic tool in process design by reducing operating costs, decreasing the use of chemical processing and, consequently, meeting the global demand for clean technologies. Keywords Protease · Immobilization · Materium 540 · Enzyme · Purification
Introduction Since the advent of enzymology, enzymes have been widely used in industrial activities such as textiles, pharmaceuticals, leather, food and detergents (Razzaq et al. 2019). According to estimates, the global industrial enzyme market will grow by 4.9% and reach US $ 7.0 billion—by 2023 (Dewan 2018). This growth can be associated with the gradual adaptation of industrial-scale production processes over the years, based on the shift from chemical to enzymatic processes to manufacture goods and commodities (Vashist et al. 2019). The wide biochemical diversity of microorganisms, * Sandra Aparecida de Assis [email protected] 1
Enzymology and Fermentation Technology Laboratory, Health Department, State University of Feira de Santana, Av Transnordestina, km 0, BR 116, Feira de Santana, BA 44036‑900, Brazil
2
DREAMS and Faculty of Engineering, Lusófona University, Lisbon, Portugal
3
Department of Bioengineering, IBB-Institute for Bioengineering and Biosciences, Instituto Superior Técnico, University of Lisbon, Lisbon, Portugal
in association with large-scale production feasibility, are the main factors turning microorganisms into the most used source to produce industrial enzymes (Dewan 2018). Besides, enzymes have been increasingly used in several industries; thus, it is important finding new microbial isolates capable of producing enzymes to meet this growing demand (Banerjee and Kumar 2
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