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Studies on growth kinetics and plasmid stability of a recombinant Escherichia coli expressing a Schistosoma mansoni antigen (1999)

Chaves, A. C. ; Abath, F. G. C. ; Lima-Filho, J. L. ; [et al.]

Springer

Bioprocess engineering 21 (1999), S. 355-361

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ISSN: 0178-515X

Keywords: Abbreviations LB ; Lurian-Bertani medium; PBS ; phosphate-buffered saline pH 7.4; IPTG ; isopropil-6-D-thiogalactoside; MBP-rSm13 ; maltose binding protein-recombinant Sm13 fusion protein; SDS-PAGE ; sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

Source: Springer Online Journal Archives 1860-2000

Topics: Process Engineering, Biotechnology, Nutrition Technology

Notes: Abstract A 13 kDa Schistosoma mansoni tegumental antigen (Sm13) was cloned and expressed in Escherichia coli. The fermentation product of 55 kDa corresponds to the maltose binding protein-recombinant Sm13 fusion protein (MBP-rSm13). The growth conditions for maximum IPTG inducible MBP-rSm13 production was investigated by examining the following parameters: innoculum size, agitation, temperature of induction and concentration of the inducer, IPTG. The maximum MBP-rSm13 production was achieved by two steps-fermentation. First, the recombinant strain was cultivated in a 37 °C orbital shaker, at 160 rpm, for 3 hours. The MBP-rSm13 was then induced by adding 0.3 mM IPTG and placing the culture in a 28 °C orbital shaker for 2 hours. Under these conditions the MBP-rSm13 production yield was approximately 50% of total intracellular proteins and the degradation by bacterial intracellular proteases seemed to be minimized. The plasmid stability was also studied during the fermentation of the Sm13-expressing E. coli in non induced and induced conditions. In both conditions there was a slightly plasmid loss before induction, however after the addition of IPTG the loss was increased. The rate of plasmid loss was 5.5 and 13.5 before and after IPTG induction respectively.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/PL00009079

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Activity and stability of an entrapped-cell system for the Δ1-dehydrogenation of steroids in organic media (1992)

Pinheiro, H. M. ; Cabral, J. M. S.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 40 (1992), S. 1123-1127

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ISSN: 0006-3592

Keywords: steriod Δ1-dehydrogenation ; immobilization ; Arthrobacter simplex ; polyurethane ; organic media ; thermostability ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Whole Arthrobacter simplex cells entrapped in κ-carra-geenan or in two types of polyurethane foam, or adsorbed on silanized Celite, were tested for the Δ1-dehydrogenation of hydrocortisone and its derivatives in organic media. Catalytic activity and stability levels were evaluated for the immobilized cells in buffer with 2.5% (vol/vol) methanol, and in three buffer-saturated solvents (n-octan-1-ol, n-decan-1-ol, and chloroform). The addition of glutamate to the immobilization support stabilized the activity of the immobilized cells in the tested organic media. The system with polyurethane (HYPOL6100)-entrapped cells (with coimmobilized glutamate) in n-decan-1-ol provided the highest long-term activity levels. Several factors involved in the polyurethane-entrapment procedure were also studied. © 1992 John Wiley & Sons, Inc.

Additional Material: 4 Ill.