Design of operational temperature for immobilized glucose isomerise using an accelerated inactivation method

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Thermal inactivation of immobilized glucose isomerase in a concentrated glucose solution was investigated in the batch mode and temperature range of 83–95 °C, which is substantially higher than the temperature used in the industrial production of high-fructose corn syrup. Simultaneous evaluation of all inactivation data showed that first-order kinetics with the Arrhenius temperature dependence of the rate constant provided a good approximation of the biocatalyst stability under the investigated conditions. The model parameters were then used to predict the operational temperature for this biocatalyst in the production of high-fructose corn syrup based on the set operational life-time of the biocatalyst. The simulation predicted a window of operational temperature of 60–65 °C, which corresponds very well with the industrial applications of this biocatalyst. This observation demonstrates that the multi-temperature method of enzyme inactivation can provide a good estimate of biocatalyst process stability and is thus a useful tool in the development of biocatalytic processes.

Anonymous (2018) Global High Fructose Corn Syrup Market Report by Type (HFCS 42, HFCS 55, HFCS 65 and HFCS 90), by End-Use Industry (Food Industry, Beverage Industry, Pharmaceuticals and Others) and by Geography – Trends and Forecast to 2025. Seattle, Coherent Market Insights. Report No. 1227.

Bandlish RK, Hess JM, Epting KL, Vieille C, Kelly RM (2002) Biotechnol. Bioeng. 80: 185–194.

Bhosale SH, Rao MB, Deshpande VV (1996) Microbiol. Rev. 60: 280.

Borgi MA, Srih-Belguith K, Ben Ali M, Mezghani M, Tranier S, Haser R, Bejar S (2004) Biochimie 86: 561–568.

Converti A, Del Borghi M (1997) Enzyme Microb. Technol. 21: 511–517.

Converti A, Del Borghi M (1998) Bioprocess Eng. 18: 27–33.

Daniel RM, Danson MJ, Eisenthal R (2001) Trends Biochem. Sci. 26: 223–225.

DiCosimo R, McAuliffe J, Poulose AJ, Bohlmann G (2013) Chem. Soc. Rev. 42: 6437–6474.

Gibbs PR, Uehara CS, Neunert U, Bommarius AS (2005) Biotechnol. Prog. 21: 762–774.

Illeová V, Polakovič M, Štefuca V, Ačai P, Juma M (2003) J. Biotechnol. 105: 235–243.

Lim LH, Saville BA (2007) Appl. Biochem. Biotechnol. 137: 115–130.

Polakovič M, Bryjak J (2002) J. Mol. Catal. B 19–20: 443–450.

Volkin DB, Klibanov AM (1989) Biotechnol. Bioeng. 33: 1104–1111.

Vrábel P, Polakovič M, Godó Š, Báleš V, Dočolomanský P, Gemeiner P (1997) Enzyme Microb. Technol. 21: 196–202.

Vrábel P, Polakovič M, Štefuca V, Báleš V (1997) Enzyme Microb. Technol. 20: 348–354.

Zittan L, Poulsen PB, Hemmingsen SH (1975) Starch/Stärke 27: 236–241.

Acta Chimica Slovaca

The Journal of Slovak University of Technology in Bratislava

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