Kinetic behaviour and thermal inactivation of pectinlyase used in food processing

Ortega, Natividad; Diego, S. de; Rodríguez‐Nogales, José Manuel; Pérez-Mateos, M.; Busto, María D.

doi:10.1111/j.1365-2621.2004.00822.x

Cited by 45 publications

(31 citation statements)

References 43 publications

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“…The activation energy (E a ) for the thermal denaturation of the purified enzyme was 26 kJ/mol (data not shown), which was similar to the value reported in the literature for the preparation Rapidase C80 (Ortega et al 2004) and also for the PG from another R. oryzae (27.2 kJ/mol) (Manjon et al 1992).…”

Section: )supporting

confidence: 73%

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Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

et al. 2012

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An acidic polygalacturonase (PG) secreted by Rhizopus oryzae MTCC-1987 in submerged fermentation condition has been purified to electrophoretic homogeneity using ammonium sulphate fractionation and anion exchange chromatography on diethylaminoethyl cellulose. The purified enzyme gave a single protein band in sodium dodecyl sulphatepolyacrylamide gel electrophoresis analysis with a molecular mass corresponding to 75.5 kDa. The Km and kcat values of the PG were 2.7 mg/mL and 2.23 × 10 3 s −1 , respectively, using citrus polygalacturonic acid as the substrate. The optimum pH of the purified PG was 5.0 and it does not loose activity appreciably if left for 24 hours in the pH range from 5.0 to 12.0. The optimum temperature of purified enzyme was 50• C and the enzyme does not loose activity below 30• C if exposed for two hours. The purified enzyme showed complete inhibition with 1 mM Ag + , Hg 2+ and KMnO4, while it was stimulated to some extent by Co 2+ . The purified PG exhibited retting of Crotalaria juncea fibre in absence of ethylenediaminetetraacetic acid.

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Section: )supporting

confidence: 73%

“…• C. Similar temperature optima for two commercial PGs, namely Pectinase CCM and Pectinex 3XL have been reported (Ortega et al 2004). Several fungal PGs exhibit temperature optima between 40-60 • C (Devi et al 1996;Kaur et al 2004;Tari et al 2008;Thakur et al 2010).…”

Section: )mentioning

confidence: 63%

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

et al. 2012

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“…However, if large values of ΔH # are coupled with a large increase in the values of ΔS # , a destabilising effect could be expected. This occurs since the increase of ΔS # compensates the high inactivation barrier, causing ΔG # to be low enough, resulting in an overall less energy requirement for the inactivation process to proceed relatively fast [49,50].…”

Section: Resultsmentioning

confidence: 98%

“…[10][11][12]. ΔG # is a measure of the spontaneity of the inactivation process, depending on ΔH # (heat change) and ΔS # (entropy change) for inactivation, which provide a measure of the number of non-covalent bonds to be broken during inactivation, and the disorder change of molecules in the system, respectively [48,49]. Positive ΔH # values indicate the endothermic character of the inactivation process [38].…”

Section: Resultsmentioning

confidence: 99%

Kinetic Stability Modelling of Keratinolytic Protease P45: Influence of Temperature and Metal Ions

Daroit

Sant’Anna

Brandelli

2011

Appl Biochem Biotechnol

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The activity and kinetic stability of a keratinolytic subtilisin-like protease from Bacillus sp. P45 was investigated in 100 mM Tris-HCl buffer (pH 8.0; control) and in buffer with addition of Ca(2+) or Mg(2+) (1-10 mM), at different temperatures. Addition of 3 mM Ca(2+) or 4 mM Mg(2+) resulted in a 26% increment on enzyme activity towards azocasein when compared to the control (100%; without added Ca(2+) or Mg(2+)) at 55 °C. Optimal temperature for activity in the control (55 °C) was similar with Mg(2+); however, temperature optimum was increased to 60 °C with 3 mM Ca(2+), displaying an enhancement of 42% in comparison to the control at 55 °C. Stability of protease P45 in control buffer and with Mg(2+) addition was assayed at 40-50 °C, and at 55-62 °C with Ca(2+) addition. Data were fitted to six kinetic inactivation models, and a first-order equation was accepted as the best model to describe the inactivation of protease P45 with and without metal ions. The kinetic and thermodynamic parameters obtained showed the crucial role of calcium ions for enzyme stability. As biocatalyst stability is fundamental for commercial/industrial purposes, the stabilising effect of calcium could be exploited aiming the application of protease P45 in protein hydrolysis.

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“…30 According to Ortega et al, 35 the H value can be correlated with the number of non-covalent broken bonds during the process of protein denaturation. Therefore, the higher H is, the larger will be the number of non-covalent bonds present in the protein molecule, which is going to be more stable.…”

Section: Inactivation Kineticmentioning

confidence: 99%

Kinetics of thermal inactivation of transglutaminase from a newly isolated Bacillus circulans BL32

Souza

Faccin

Mertins

et al. 2009

J of Chemical Tech & Biotech

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BACKGROUND: This paper describes the modeling of the kinetics of thermal inactivation of transglutaminase (TGase) from a newly isolated Bacillus circulans BL32, isolated from the Amazon environment. The purified enzyme was incubated at temperatures ranging from 30 to 70• C and values of the thermodynamic inactivation parameters, such as activation energy ( E), activation enthalpy ( H), activation entropy ( S), and free energy ( G) for thermal inactivation, were calculated.

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Kinetic behaviour and thermal inactivation of pectinlyase used in food processing

Cited by 45 publications

References 43 publications

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre

Kinetic Stability Modelling of Keratinolytic Protease P45: Influence of Temperature and Metal Ions

Kinetics of thermal inactivation of transglutaminase from a newly isolated Bacillus circulans BL32

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