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The Constitutive Production of Pectinase by the CT1 Mutant of Penicillium Occitainis is Modulated by pH

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Abstract

The aim of the present study was to investigate pectinases production by CT1 mutant of Penicillium occitanis on glucose based media. Two main groups of pectinases were followed: lyases (pectin and pectate lyases) and hydrolases (polygalacturonases and polymethylgalacturonases). When cultivated in different liquid media, where either the starting glucose concentration or the nature of nitrogen sources used was varied, the CT1 mutant secreted either lyases or hydrolases. In fact, the pH of these various media seemed to correlate with the activity produced: The lyases were highly and exclusively produced at neutral or alkaline ambient pH, whereas hydrolases were highly produced on acidic ambient pH. Such conclusion was confirmed by following pectinase production in the same culture medium (with the same glucose concentration and the same nitrogen source) set at two initial pH of 4 and 7. Altogether, these results suggest that the pectinases control by PacC signaling pathway of P. occitanis should resemble to that of Aspergillus and its ability to “activate the expression of alkaline-expressed genes and repress acid-expressed genes” remains intact in the CT1 over-producing and constitutive strain. Enzymes produced at acidic pH (hydrolases) and at neutral pH (lyases) were applied in the hydrolysis of orange peel and gave results comparable to commercial enzymes.

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Acknowledgments

We extend our gratitude to Mr. Aouar Smaoui, from the English department at the Sfax Faculty of Science for carefully proofreading, reviewing and editing the manuscript of the current paper. This work is supported by the « Ministère de l’Enseignement Supérieur, de la Recherche Scientifique et de la Technologie ».

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Correspondence to Ali Gargouri.

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Romdhane, Z.B., Tounsi, H., Hadj-Sassi, A. et al. The Constitutive Production of Pectinase by the CT1 Mutant of Penicillium Occitainis is Modulated by pH. Appl Biochem Biotechnol 169, 215–227 (2013). https://doi.org/10.1007/s12010-012-9971-6

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  • DOI: https://doi.org/10.1007/s12010-012-9971-6

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