Analysis of mechanism and kinetics of thermal inactivation of enzymes: Evaluation of multitemperature data applied to inactivation of yeast invertase

Vrábel, Peter; Polakovič, Milan; Štefuca, Vladimı́r; Báleš, V.

doi:10.1016/s0141-0229(96)00150-0

Cited by 48 publications

(22 citation statements)

References 31 publications

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“…It has been previously published that deactivation of the external invertase follows biphasic kinetic (Cavaille & Combes, 1995;Rodriguez et al, 1997;Vrabel, Polakovič, Štefuca, & Baleš, 1997). Our obtained results implied that the cause of biphasic kinetics of denaturation could be caused by the existence of the four isoforms in the preparations of external invertase.…”

Section: Thermal Stabilitysupporting

confidence: 66%

Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms

2010

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Section: Thermal Stabilitysupporting

confidence: 66%

Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms

2010

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“…Other methods are based either on the presumption that the kinetics obeys the MichaelisMenten model [5], the inactivation parameters being obtained from the values of Michaelis constant, or by using specific [2,6] or phenomenological models [7] that leads to certain definite kinetic equations.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Oancea

Stuparu

Nita

et al. 2008

Biophysical Chemistry

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Please cite this article as: D. Oancea, Alexandrina Stuparu, Madalina Nita, Mihaela Puiu, Adina Raducan, Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method, Biophysical Chemistry (2008Chemistry ( ), doi: 10.1016Chemistry ( /j.bpc.2008 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. A C C E P T E D M A N U S C R I P T ACCEPTED MANUSCRIPT ABSTRACTAn isoconversional method is proposed in order to calculate the kinetic parameters of enzyme inactivation. The method provides an efficient and low-cost procedure to describe both operational and thermal inactivation. Unlike the ordinary kinetic assays performed at constant enzyme concentration and at various substrate concentrations, the isoconversional method requires several extended kinetic curves for constant initial substrate concentration and different enzyme concentrations. The procedure was tested and validated using simulated data obtained for several kinetic models frequently discussed in the literature. After the validation, the isoconversional method was used for the investigation of the thermoinactivation of urease during urea hydrolysis in self buffered medium and the operational inactivation (destructive oxidation by excess peroxide) of catalase at high concentration of hydrogen peroxide. The results showed that the isoconversional method gives good results of global inactivation constant for both simple and more complex models.

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“…An appropriate incubation period is of critical importance for invertase synthesis, as longer incubation can cause feedback repression of the enzyme (Vrabel et al 1997;Gomez et al 2000). In this manuscript, we report the isolation of Saccharomyces cerevisiae for the production of invertase and kinetic analysis of shake flask fermentation.…”

Section: Introductionmentioning

confidence: 99%

Effect of cultivation conditions on invertase production by hyperproducing Saccharomyces cerevisiae isolates

Haq

Baig

Ali

2005

World J Microbiol Biotechnol

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Invertase (b-D-fructofuranoside fructohydrolase, EC 3.2.1.26) finds major uses in confectionery and in the production of invert syrup. In the present study, we report on invertase production by wild cultures of Saccharomyces cerevisiae. The yeast strains were isolated from dates available in a local market. Five hyperproducing yeast strains (>100-fold higher invertase activity) were kinetically analysed for invertase production. Saccharomyces cerevisiae strain GCA-II was found to be a better invertase-yielding strain than all the other isolates. The values of Q p and Y p/s for GCA-II were economical as compared to other Saccharomyces cultures. The effect of sucrose concentration, rate of invertase synthesis, initial pH of fermentation medium and different organic nitrogen sources on the production of invertase under submerged culture conditions was investigated. Optimum concentrations of sucrose, urea and pH were 3, 0.2 (w/v), and 6 respectively. The increase in the enzyme yield obtained after optimization of the cultural conditions was 47.7%.

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Analysis of mechanism and kinetics of thermal inactivation of enzymes: Evaluation of multitemperature data applied to inactivation of yeast invertase

Cited by 48 publications

References 31 publications

Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms

Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms

Estimation of the overall kinetic parameters of enzyme inactivation using an isoconversional method

Effect of cultivation conditions on invertase production by hyperproducing Saccharomyces cerevisiae isolates

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