MALDI-TOF MS and ESI-LTQ-Orbitrap tandem mass spectrometry reveal specific porphyranase activity from a Pseudoalteromonas atlantica bacterial extract - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue RSC Advances Année : 2015

MALDI-TOF MS and ESI-LTQ-Orbitrap tandem mass spectrometry reveal specific porphyranase activity from a Pseudoalteromonas atlantica bacterial extract

Résumé

A better understanding of the chemical–physical properties of porphyran – a complex anionic polysaccharide – and the development of potential industrial applications requires more in-depth knowledge of its structural organization. The structural complexity of the hybrid (co-polymer) structure of porphyran stems from the co-occurrence of two repetition moieties LA-G and L6S-G, which can be methylated on the D-galactose. The enzymes currently available for the structural analyses of porphyran are limited in specificity, and methylated porphyran cannot be digested by previously described β-porphyranases. Here, MALDI-TOF MS analysis and tandem ESI-MS sequencing of porphyran degradation products after incubation with protein extracts from the marine bacterium Pseudoalteromonas atlantica revealed methylated disaccharide (L6S-GMe) and dimethylated tetrasaccharide (L6S-GMe–L6S-GMe) end-products that have never been described before. Our results highlighted unprecedented β-methyl-porphyranase activity that can accommodate the methylated building blocks of porphyran.
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Dates et versions

hal-01966791 , version 1 (29-12-2018)

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C. Przybylski, G. Correc, M. Fer, F. Gonnet, W. Helbert, et al.. MALDI-TOF MS and ESI-LTQ-Orbitrap tandem mass spectrometry reveal specific porphyranase activity from a Pseudoalteromonas atlantica bacterial extract. RSC Advances, 2015, 5 (98), pp.80793-80803. ⟨10.1039/C5RA14449C⟩. ⟨hal-01966791⟩
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