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Abstract
The bacterium Pseudomonas fluorescens 07A produces a protease with potential for industrial application. In order to remedy problems associated with the use of free enzymes and allow its reuse, the protease was immobilized on DEAE Sephacel® resin via three different strategies based on ionic interaction and covalent bonding. The matrix-bound enzymes were characterized in relation to their activity (pH, temperature and stability), reuse and storage. Immobilization raised the optimum temperature of activity from 37 °C to 50 °C, whereas the pH of highest activity changed from 7.5 to 7.0 or 8.0, depending on the immobilization strategy. Immobilization proved to be efficient for successive reuses, even leading to an increase in the enzymatic activity along the use. The immobilized enzyme also presented greater stability to high temperatures and storage conditions and has potential as a biocatalyst for industrial applications due to its high efficiency, stability and easy recovery.
Highlights
IntroductionThe enzyme is physically or chemically associated with a support through interactions or entrapment (Khan et al 2017; Kumari and Kayastha 2011; Shrinivas et al 2012)
Proteases hydrolyze peptide bonds, being widely used in the food and pharmaceutical industries (Kumar and Takagi 1999), such as for beverage clarification and production of Kimberly Freitas Cardoso and Juliana Severo Miranda have contributed to this paper.During immobilization, the enzyme is physically or chemically associated with a support through interactions or entrapment (Khan et al 2017; Kumari and Kayastha 2011; Shrinivas et al 2012)
The low immobilization efficiency found for the three strategies is probably due to the effects of mass transfer when using a porous matrix, leading to a resistance for the substrate diffusion inside the support, which results in lower enzymatic activity
Summary
The enzyme is physically or chemically associated with a support through interactions or entrapment (Khan et al 2017; Kumari and Kayastha 2011; Shrinivas et al 2012). This process promotes changes in the catalytic properties and allows the reuse of the enzyme, reducing costs (Mehdi et al 2017; Shi et al 2010). Physical immobilizations using ion exchange resins are based on the interaction between negatively or positively charged groups of the matrix and charged residues on the enzyme. Ion exchange immobilization presents limited application due to the possibility of desorption of the enzyme during its use, which can be minimized by crosslinking the
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