About: Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis

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About: Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis
Creator	Fraaije, Marco Janssen, Dick Van Bloois, Edwin Winter, Remko
Source	PMC
abstract	Streptomyces coelicolor A3(2) alditol oxidase (AldO) is a soluble monomeric flavoprotein in which the flavin cofactor is covalently linked to the polypeptide chain. AldO displays high reactivity towards different polyols such as xylitol and sorbitol. These characteristics make AldO industrially relevant, but full biotechnological exploitation of this enzyme is at present restricted by laborious and costly purification steps. To eliminate the need for enzyme purification, this study describes a whole-cell AldO biocatalyst system. To this end, we have directed AldO to the periplasm or cell surface of Escherichia coli. For periplasmic export, AldO was fused to endogenous E. coli signal sequences known to direct their passenger proteins into the SecB, signal recognition particle (SRP), or Twin-arginine translocation (Tat) pathway. In addition, AldO was fused to an ice nucleation protein (INP)-based anchoring motif for surface display. The results show that Tat-exported AldO and INP-surface-displayed AldO are active. The Tat-based system was successfully employed in converting xylitol by whole cells, whereas the use of the INP-based system was most likely restricted by lipopolysaccharide LPS in wild-type cells. It is anticipated that these whole-cell systems will be a valuable tool for further biological and industrial exploitation of AldO and other cofactor-containing enzymes.
has issue date	2009-06-01(xsd:dateTime)
bibo:doi	10.1007/s00253-009-1904-0
bibo:pmid	19224207
has license	no-cc
sha1sum (hex)	5d52ca29c83f7115aa277b5b2c369a12b74577cf
schema:url	https://doi.org/10.1007/s00253-009-1904-0
resource representing a document's title	Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis
has PubMed Central identifier	PMC2690846
has PubMed identifier	19224207
schema:publication	Appl Microbiol Biotechnol
resource representing a document's body	covid:5d52ca29c83f7115aa277b5b2c369a12b74577cf#body_text
is schema:about of	named entity 'AldO' named entity 'AldO' named entity 'AldO' named entity 'polyols' named entity 'motif' named entity 'Streptomyces' named entity 'ALDITOL' named entity 'HAVE' named entity 'LPS' named entity 'TAT' named entity 'BUT' named entity 'FUSED TO' named entity 'STUDY' named entity 'TRANSLOCATION' named entity 'END' named entity 'BASED' named entity 'SECB' named entity 'STEPS' named entity 'SEQUENCES' covid:arg/5d52ca29c83f7115aa277b5b2c369a12b74577cf named entity 'biocatalyst' named entity 'enzyme' named entity 'flavoprotein' named entity 'These' named entity 'active' named entity 'lipopolysaccharide' named entity 'direct' named entity 'surface' named entity 'study' named entity 'cell' named entity 'xylitol' named entity 'polypeptide chain' named entity 'enzyme' named entity 'biocatalyst' named entity 'xylitol' named entity 'signal sequences' named entity 'endogenous' named entity 'nucleation' named entity 'enzyme' named entity 'E. coli' named entity 'wild-type' named entity 'Streptomyces coelicolor' named entity 'biocatalysis' named entity 'periplasm' named entity 'oxidase' named entity '0.01' named entity 'conformation' named entity 'cell surface' named entity 'FAD' named entity 'proteinase' named entity 'antisera' named entity 'riboflavin' named entity 'wild-type' named entity 'substrates' named entity 'kanamycin' named entity 'cofactor' named entity 'GFP' named entity 'Tris-buffered saline' named entity 'E. coli' named entity 'cellular localization' named entity 'biocatalysis' named entity 'polyols' named entity 'E. coli' named entity 'nucleation' named entity 'SRP' named entity 'outer membrane' named entity 'ampicillin' named entity 'mature protein' named entity 'riboflavin' named entity 'protein' named entity 'wild-type' named entity 'enzyme' named entity 'DsbA' named entity 'glycosylphosphatidylinositol (GPI) anchor' named entity 'FAD' named entity 'Invitrogen' named entity 'E. coli' named entity 'signal sequence'

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