Secretory production of an FAD cofactor‐containing cytosolic enzyme (sorbitol–xylitol oxidase from S treptomyces coelicolor ) using the twin‐arginine translocation ( Tat ) pathway of C orynebacterium glutamicum

Carbohydrate oxidases are biotechnologically interesting enzymes that require a tightly or covalently bound cofactor for activity. Using the industrial workhorse C orynebacterium glutamicum as the expression host, successful secretion of a normally cytosolic FAD cofactor‐containing sorbitol–xylitol...

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Veröffentlicht in:Microbial biotechnology 2013-03, Vol.6 (2), p.202-206
Hauptverfasser: Scheele, Sandra, Oertel, Dan, Bongaerts, Johannes, Evers, Stefan, Hellmuth, Hendrik, Maurer, Karl‐Heinz, Bott, Michael, Freudl, Roland
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Sprache:eng
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Zusammenfassung:Carbohydrate oxidases are biotechnologically interesting enzymes that require a tightly or covalently bound cofactor for activity. Using the industrial workhorse C orynebacterium glutamicum as the expression host, successful secretion of a normally cytosolic FAD cofactor‐containing sorbitol–xylitol oxidase from S treptomyces coelicolor was achieved by using the twin‐arginine translocation ( Tat ) protein export machinery for protein translocation across the cytoplasmic membrane. Our results demonstrate for the first time that, also for cofactor‐containing proteins, a secretory production strategy is a feasible and promising alternative to conventional intracellular expression strategies.
ISSN:1751-7915
1751-7915
DOI:10.1111/1751-7915.12005