Thermal Inactivation Kinetics of Peroxidase in Coriander Leaves

Rudra, Shalini Gaur; Shivhare, U. S.; Basu, Santanu; Sarkar, B. C.

doi:10.1007/s11947-007-0013-2

Cited by 29 publications

(16 citation statements)

References 30 publications

(38 reference statements)

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“…varied between 0.007 and 0.107. These values are comparable [13,15,21,36]. Hence, among the mathematical models evaluated, the first order was accepted as the best equation to describe the inactivation of protease P45 in the conditions employed.…”

Section: Resultsmentioning

confidence: 96%

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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Section: Resultsmentioning

confidence: 96%

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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“…It was defined in this study as the half-life (t 1/2 ), since it includes the contribution of the deactivation rate constants k 1 and k 2 and the residual activity α 1 . As it was the case for inactivation of peroxidase at temperatures lower than 90°C (Rudra et al 2008), inactivation of soluble and immobilized GA followed the series type inactivation model (R 2 >0.99, Eq. 5), and the kinetic constant k 1 was significantly larger than k 2 .…”

Section: Properties Of Ga Bone Derivativementioning

confidence: 91%

Bone-Bound Glucoamylase as a Biocatalyst in Bench-Scale Production of Glucose Syrups from Liquefied Cassava Starch

Carpio

Escobar

Batista‐Viera

et al. 2008

Food Bioprocess Technol

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This research assesses the bench-scale application of a non-conventional support, bone particles, for glucoamylase (GA) immobilization and its subsequent use in cassava starch hydrolysis. Upon determining the appropriate conditions to immobilize GA onto chicken bone particles, such as pH, ionic strength, particle size, and enzyme load, bench-scale immobilization of commercial GA without further purification was performed. Under the selected conditions, 270 GA units per gram of support were adsorbed. Optimal temperature and thermal stability of immobilized GA were only slightly different from those of the free enzyme, while optimal pH became more acidic by about one unit. The feasibility of the use of this immobilized biocatalyst for high glucose syrup production from liquefied cassava starch, at bench scale in batch process using a stirred-tank reactor, was demonstrated. Repeated use of the GA-bone derivative showed that similar conversions to those achieved with soluble enzyme (dextrose equivalent=98) were reached until the third batch and over 90% until the 25th batch.

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“…However, thermal inactivation of peroxidase at temperatures not exceeding 80-90°C has been observed as a biphasic process with different rate constants (Rudra et al 2008); this behavior is also followed by other enzymes (Polakovič and Vrábel 1996), such as GA (Polakovič and Bryjak 2002). The deviation from the first-order kinetics has been attributed to the presence of some isoenzymes of different thermal stabilities (Rudra et al 2008).…”

Section: Effect Of Immobilization Process On Ga Propertiesmentioning

confidence: 99%

Improved Glucoamylase Immobilization onto Calcined Chicken Bone Particles

Carpio

Batista‐Viera

Ruales

2009

Food Bioprocess Technol

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Calcination was considered for the first time as an alternative to recover inorganic bone component from spent glucoamylase-bone derivatives. The subsequent adsorption of glucoamylase (GA) onto calcined bone particles was assessed. Adsorption capacity of the calcined matrix was found to be from 1.1-to 1.4-fold superior to that of non-calcined supports, and it was dependent on the applied load. Moreover, the expressed activity of GA derivatives on calcined matrix was, at least, 2-fold higher than that of biocatalysts onto non-calcined support. The optimization of the loading allowed the preparation of derivatives with 139 GA units per gram of support, which preserve 52% of the immobilized activity. Additionally, calcination of spent GA biocatalysts on calcined bone particles was performed, and adsorption of glucoamylase onto the bone particles calcined a second time was also found to be efficient. In addition to the improved catalytic properties, the half-life at 55°C of the GA biocatalysts on calcined bone was increased 1.7-fold in comparison with that of soluble GA and GA adsorbed onto non-calcined bone particles. Furthermore, the same cassava starch conversion can be achieved batchwise in a stirred-tank reactor using less insoluble biocatalyst, 37% of the GA-bone derivative, which represents an important saving for industrial applications. Nomenclature B 203Bone support with an average particle size of 203 µm calB 203 Support produced by B 203 calcination at 550°C DB 203 GA derivative on B 203 calDB 203 Support recovered from DB 203 by calcination at 550°C and further classification by sifting and mixing of fractions in the same ratio as B 203 2 nd calDB 203 Support recovered by a second calcination at 550°C from used calDB 203 B 360 Bone matrix with an average particle size of 360 µm calB 360 Matrix made by B 360 calcination at 550°C HA Hydroxy-or hydroxilapatite calHA HA calcined at 550°C DHA Derivative on HA DE Total amount of reducing sugars expressed as dextrose, calculated as a percentage of the total solids

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Thermal Inactivation Kinetics of Peroxidase in Coriander Leaves

Cited by 29 publications

References 30 publications

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

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

Bone-Bound Glucoamylase as a Biocatalyst in Bench-Scale Production of Glucose Syrups from Liquefied Cassava Starch

Improved Glucoamylase Immobilization onto Calcined Chicken Bone Particles

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