Purification of chondroitin precursor from Escherichia coli K4 fermentation broth using membrane processing

2011 ◽  
Vol 6 (4) ◽  
pp. 410-419 ◽  
Author(s):  
Chiara Schiraldi ◽  
Immacolata Loredana Carcarino ◽  
Alberto Alfano ◽  
Odile Francesca Restaino ◽  
Andrea Panariello ◽  
...  
RSC Advances ◽  
2016 ◽  
Vol 6 (86) ◽  
pp. 82571-82580 ◽  
Author(s):  
Muhammad Hakimi Hadzir ◽  
Sahar Abbasiliasi ◽  
Arbakariya B. Ariff ◽  
Siti Baidurah Yusoff ◽  
Hui Suan Ng ◽  
...  

Evaluations of ILATPSs were performed with a variety of ionic liquids and salts as phase components to figure out their competencies in the recovery of lipase from a fermentation broth of E. coli using banana waste as a substrate.


2010 ◽  
Vol 150 ◽  
pp. 82-82
Author(s):  
D. Cimini ◽  
E. Carlino ◽  
O.F. Restaino ◽  
R. De Mattia ◽  
M. De Rosa ◽  
...  

2009 ◽  
Vol 85 (6) ◽  
pp. 1779-1787 ◽  
Author(s):  
Donatella Cimini ◽  
Odile Francesca Restaino ◽  
Angela Catapano ◽  
Mario De Rosa ◽  
Chiara Schiraldi

1996 ◽  
Vol 313 (2) ◽  
pp. 589-596 ◽  
Author(s):  
Helgi H. HANNESSON ◽  
Åsa HAGNER-McWHIRTER ◽  
Kerstin TIEDEMANN ◽  
Ulf LINDAHL ◽  
Anders MALMSTRÖM

The capsular polysaccharide from Escherichia coli K4 consists of a chondroitin {[GlcA(β1→3)GalNAc(β1→4)]n} backbone, to which β-fructofuranose units are linked to C-3 of D-glucuronic acid (GlcA) residues. Removal of the fructose units by mild acid hydrolysis provided a substrate for the GlcA C-5 epimerase, which is involved in the generation of L-iduronic acid (IdoA) units during dermatan sulphate biosynthesis. Incubation of this substrate with solubilized fibroblast microsomal enzyme in the presence of 3H2O resulted in the incorporation of tritium at C-5 of hexuronyl units. A Km of 67×10-6 M hexuronic acid (equivalent to disaccharide units) was determined, which is similar to that (80×10-6 M) obtained for dermatan (desulphated dermatan sulphate). Vmax. was about 4 times higher with dermatan than with the K4 substrate. A defructosylated K4 polysaccharide isolated after incubation of bacteria with D-[5-3H]glucose released 3H2O on reaction with the epimerase, and thus could be used to assay the enzyme. Incubation of a K4 substrate with solubilized microsomal epimerase for 6 h in the presence of 3H2O resulted in the formation of about 5% IdoA and approximately equal amounts of 3H in GlcA and IdoA. A corresponding incubation of dermatan yielded approx. 22% GlcA, which contained virtually all the 3H label. These results are tentatively explained in terms of a two-base reaction mechanism, involving a monoprotic L-ido-specific base and a polyprotic D-gluco-specific base. Most of the IdoA residues generated by the enzyme occurred singly, although some formation of two or three consecutive IdoA-containing disaccharide units was observed.


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