Production of sorbitol and gluconic acid by permeabilized cells of Zymomonas mobilis

Rehr, Bert; Wilhelm, Cornelia; Sahm, Hermann

doi:10.1007/bf00184677

Cited by 76 publications

(26 citation statements)

References 20 publications

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“…By this procedure, larger pores were opened in the cell wall to allow an easier access of substrates to GFOR/GL, but the enzymes still remained in cell periplasm (8). As shown in Table 3, with Table 3.…”

Section: Resultsmentioning

confidence: 99%

“…The pH was automatically controlled at 6.4 by adding 10M NaOH and the temperature was 39ºC. Cell permeabilisation was done by treating concentrated Z. mobilis suspensions with cetyltrimethylammonium bromide (CTAB) as described by Rehr et al (8).…”

Section: Bioconversion Of Glucose and Fructose To Gluconic Acid And Smentioning

confidence: 99%

“…Some processes for producing sorbitol and gluconic acid have been proposed in which, instead of purified enzymes, previously grown, concentrated, and permeabilised Z. mobilis cells were used (3,8). The reason for the permeabilisation of cells was to release essential soluble co-factors needed for the conversion of both glucose and gluconate to ethanol and other catabolic products.…”

Section: Introductionmentioning

confidence: 99%

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Activity of glucose-fructose oxidoreductase in fresh and permeabilised cells of Zymomonas mobilis grown in different glucose concentrations

Erzinger¹,

Silveira²,

Costa³

et al. 2003

Braz. J. Microbiol.

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Previously grown cells of the ethanologenic bacterium Zymomonas mobilis produce sorbitol and gluconic acid, in reactions catalysed by the periplasmic enzymes glucose-fructose oxidoreductase (GFOR) and glucono-δ-lactonase (GL). The GFOR/GL system activity, in cells to be used in this bioconversion, depends on growth conditions. In batch runs, with initial glucose concentrations (S0) from 42 to 230 g/L, the highest specific and total GFOR/GL activities were obtained with S0 = 153 g/L (12.6 U/g cells and 62 U/L). Higher S0 led to decreasing activities in fresh cells. With S0 = 209 g/L, the final specific activity was only 7.0 U/g. After disruption of cells, however, an activity over 15 U/g was revealed. Since growth inhibition with S0 over 153 g/ L was observed in batch mode, fed-batch runs, equivalent to a batch of 230 g/L, were done. Although no growth inhibition occurred in fed-batch cultivation, enzyme activity remained low (5.2 U/g). A further fedbatch experiment, carried out under low pressure to remove ethanol from the medium, resulted in a specific activity of 9.8 U/g and a total activity of 68.7 U/L. These results indicate that the low GFOR/GL activities in Z. mobilis cells grown on higher S0 were due to changes in the cell wall, caused by high concentration of ethanol, that hindered the transport of the substrate to the intracellular enzymes in biconversion runs. This conclusion was confirmed by bioconversion runs with cells cultivated under different conditions.

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Section: Resultsmentioning

confidence: 99%

Section: Bioconversion Of Glucose and Fructose To Gluconic Acid And Smentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Activity of glucose-fructose oxidoreductase in fresh and permeabilised cells of Zymomonas mobilis grown in different glucose concentrations

Erzinger¹,

Silveira²,

Costa³

et al. 2003

Braz. J. Microbiol.

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“…The enzyme is composed of four identical subunits with a molecular mass of 40 kDa, and one noncovalently bound cofactor molecule per subunit (Zachariou & Scopes, 1986). NADP(H) cannot be dissociated from the enzyme through extensive dialysis or treatment with 8 M urea (Zachariou & Scopes, 1986;Rehr et al, 1991), but is easily removed from the enzyme by low amounts (0.1070) of SDS (H. Loos, H. Sahm, & G. A. Sprenger, unpubl. results).…”

mentioning

confidence: 99%

Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis

et al. 1994

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Glucose-fructose oxidoreductase (E.C. 1. I .99.-) from the ethanol-producing Gram-negative bacterium Zyrnomonas mobilis is a periplasmic, soluble enzyme that forms a homotetramer of 1 6 0 kDa with one NADP(H) cofactor per subunit that is tightly, but noncovalently, bound. The enzyme was crystallized by the hanging drop vapor diffusion method using sodium citrate as precipitant. The obtained crystals belong to the space group P21212, with unit cell constants of 84.6 A, 94.1 A, and 117.OA, consistent with two monomers in the asymmetric unit.They diffract to a resolution of about 2 A and are suitable for X-ray structure determination.

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“…A biomassa, concentrada a 25g/L foi, em seguida, submetida à permeabilização com 0,2% (m/v) de brometo de cetil trimetil amônio (CTAB), seguindo a metodologia proposta por Rehr et al (1991) com algumas modificações.…”

Section: Produção De Células/enzimasunclassified

AVALIAÇÃO DA TEMPERATURA NA PRODUÇÃO DE ÁCIDO LACTOBIÔNICO E SORBITOL POR CÉLULAS DE Zymomonas mobilis IMOBILIZADAS EM ALGINATO DE CÁLCIO

Carra¹,

Rodrigues²,

Beraldo³

et al. 2015

Anais Do XX Congresso Brasileiro De Engenharia Química

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RESUMO:As enzimas periplasmáticas de Zymomonas mobilis glicose-frutose oxidorredutase e gluconolactonase convertem lactose em ácido lactobiônico e frutose em sorbitol. Neste sistema, células inativadas contendo as enzimas são imobilizadas para permitir sua reutilização. As enzimas são influenciadas pela temperatura, tanto com respeito à velocidade reacional quanto à termoestabilidade. O objetivo desse estudo foi avaliar a formação de produtos sob temperaturas de 36, 39, 43 e 47°C, utilizando 20g/L de células imobilizadas em alginato de cálcio, com pH de 6,4. A 43°C, maiores concentração de produtos (510mmol/L) e produtividade (21,3mmol/L/h) foram atingidos. A máxima velocidade específica de formação de produtos, no início do processo, foi favorecida com o aumento da temperatura devido ao maior fluxo de produtos e substratos pelas esferas de alginato. A 47°C, entretanto, observou-se queda acentuada na velocidade, causada, possivelmente, pela desnaturação das enzimas.

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Production of sorbitol and gluconic acid by permeabilized cells of Zymomonas mobilis

Cited by 76 publications

References 20 publications

Activity of glucose-fructose oxidoreductase in fresh and permeabilised cells of Zymomonas mobilis grown in different glucose concentrations

Activity of glucose-fructose oxidoreductase in fresh and permeabilised cells of Zymomonas mobilis grown in different glucose concentrations

Crystallization and preliminary x‐ray analysis of glucose‐fructose oxidoreductase from zymomonas mobilis

AVALIAÇÃO DA TEMPERATURA NA PRODUÇÃO DE ÁCIDO LACTOBIÔNICO E SORBITOL POR CÉLULAS DE Zymomonas mobilis IMOBILIZADAS EM ALGINATO DE CÁLCIO

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