Reference : Overproduction and properties of the mannuronate alginate lyase AlxMB
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/91710
Overproduction and properties of the mannuronate alginate lyase AlxMB
English
Malissard, Martine [Université Claude Bernard - Lyon 1 - UCLB > > Laboratoire de Biochimie Microbienne > >]
Chavagnat, Frédéric [Université Claude Bernard - Lyon 1 - UCLB > > Laboratoire de Biochimie Microbienne > > > >]
Duez, Colette mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Vacheron, Marie-Jeanne [Université Claude Bernard - Lyon 1 - UCLB > > Laboratoire de Biochimie Microbienne > > > >]
Guinand, Micheline [Université Claude Bernard - Lyon 1 - UCLB > > Laboratoire de Biochimie Microbienne > > > >]
Michel, Georges [Université Claude Bernard - Lyon 1 - UCLB > > Laboratoire de Biochimie Microbienne > > > > > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > > Centre d'ingénierie des protéines > > > > > > >]
15-Feb-1995
FEMS Microbiology Letters
Blackwell Publishing
126
2
105-111
Yes (verified by ORBi)
International
0378-1097
1574-6968
Oxford
United Kingdom
[en] amino acid sequence ; base sequence ; cloning, molecular ; escherichia coli/enzymology/genetics ; molecular sequence data ; plasmids/genetics ; polysaccharide-lyases/*biosynthesis/chemistry/genetics/isolation ; purification
[en] In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of 50 mu g per litre of culture. The polypeptide chain was cleaved between two cysteine residues, C169 and C183, themselves linked by a disulphide bridge. AlxM has now been overproduced in E. coli BL21(DE3)/pAL-Sur/pLysS. Under conditions in which formation of inclusion bodies can be avoided, the enzyme is synthesized as a catalytically active, water-soluble, unnicked polypeptide with a yield of 32 mg per litre of culture. It has been purified to protein homogeneity using a one-step procedure. The nicked ALxM(A) and unnicked ALxM(B) alginate lyases have identical alginate-degrading activities at high salt concentrations.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/91710
10.1016/0378-1097(94)00536-Z

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