Proteomic insight into the primycin fermentation process of Saccharomonospora azurea

Valasek, Andrea and Kiss, Írisz Éva and Fodor, István and Kovács, Márk and Urbán, Péter and Jámbor, Éva and Fekete, Csaba and Kerepesi, Ildikó (2016) Proteomic insight into the primycin fermentation process of Saccharomonospora azurea. Acta Biologica Hungarica, 67 (4). pp. 424-430. ISSN 0236-5383

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Abstract

Saccharomonospora azurea SZMC 14600 is a member of the family Pseudonocardiaceae exclusively used for industrial scale production of primycin a large 36-membered non-polyene macrolide lactone antibiotic belonging to the polyketide class of natural products. Even though maximum antibiotic yield has been achieved by empirically optimized two-step fermentation process, little is known about the molecular components and mechanisms underlying the efficient antibiotic production. In order to identify differentially expressed proteins (DEPs) between the pre- and main-fermentation stages of primycin, comparative 2D-PAGE experiments were performed. In total, 98 DEP spots were reproducibly detected, out of which four spots were excised from gels, and identified through MALDI-TOF/TOF mass spectrometry. Peptide mass fingerprint analysis revealed peptide matches to HicB antitoxin for the HicAB toxin-antitoxin system (EHK86651), to a nucleoside diphosphate kinase regulator ((Ndk; EHK81899) and two other proteins with unknown function (EHK88946 and EHK86777).

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