Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Lappe, Rosiele; Cladera-Olivera, Florencia; Dominguez, Ana Paula Melo; Brandelli, Adriano

doi:10.1016/j.jfoodeng.2008.08.025

Cited by 24 publications

(17 citation statements)

References 26 publications

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“…Based on the semi-log plots linear of carboxylmethylcellulase activities versus heat treatment time at temperature ranged from 50 to 65°C (Table 1), it can be concluded that thermal inactivation described a first-order reaction. These results are in agreement with those reported for peptide cerein 8A (Lappe et al, 2009) and for beta-glucosidase from the digestive juice of the land crab Cardisoma armatum (Ya et al, 2014).…”

Section: Thermal Inactivation Kinetics Of Carboxylmethylcellulasessupporting

confidence: 93%

“…With the increasing temperature, the t 1/2 decreased and showed values ranged between 67.28 ± 2.06 and 17.63 ± 0.07 min for Ab-CX1, and between 46.51 ± 1.98 and 16.65 ± 0.04 min for Ab-CX2. This would indicate that the enzymes are unstable at higher temperature (Lappe, et al, 2009). The increase in half-life by 1.6 fold for Ab-CX1 at 60°C clearly indicates that Ab-CX1 was more stable.…”

Section: Thermal Inactivation Kinetics Of Carboxylmethylcellulasesmentioning

confidence: 97%

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Kinetic and Thermodynamic Analysis of Two Carboxymethylcellulases from Macrotermes subhyalinus Little Soldier

Bedel¹,

Gnanwa²,

Kone³

et al. 2017

IJB

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Optimization of thermal processes relies on adequate degradation kinetic models to warrant food safety and quality. The knowledge on thermal inactivation of enzymes is necessary to allow their proper utilization in food industry and technology applications, enabling the reduction of heating times and optimization of heating temperatures. In this work, the kinetic of thermal inactivation was studied for the previously characterized carboxylmethylcellulases Ab-CX1 and Ab-CX2 from Macrotermes subhyalinus little soldier. Samples of carboxymethylcellulases were treated at different time-temperature combinations in the range of 5-60 min at 50-65°C and the kinetic and thermodynamic parameters for carboxymethylcellulases were calculated. Results showed that inactivation followed a first-order reaction with k-values between 0.0103 ± 0.0003 to 0.1217 ± 0.0005 and 0.0149 ± 0.0007 to 0.0416 ± 0.0003 min -1 for Ab-CX1 and Ab-CX2, respectively. At high temperatures, Ab-CX2 was less resistant, with a significant decrease in residual activity compared to Ab-CX1. The D-and k-values decreased and increased, respectively, with increasing temperature, indicating faster inactivation of carboxymethylcellulases. Activation energy (Ea) and Z-values were estimated to 76.74 ± 1.98 kJ.mol were also calculated. The high value obtained for the variation in enthalpy of activation indicates that a high amount of energy is required to initiate denaturation, probably due to the molecular conformation of carboxymethylcellulases. All results suggest that both carboxymethylcellulases are relatively resistant to long heat treatments up to 50°C.

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Section: Thermal Inactivation Kinetics Of Carboxylmethylcellulasessupporting

confidence: 93%

Section: Thermal Inactivation Kinetics Of Carboxylmethylcellulasesmentioning

confidence: 97%

Kinetic and Thermodynamic Analysis of Two Carboxymethylcellulases from Macrotermes subhyalinus Little Soldier

Bedel¹,

Gnanwa²,

Kone³

et al. 2017

IJB

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“…Thermal inactivation tests were performed as described elsewhere (Lappe, Cladera-Olivera, Dominguez, & Brandelli, 2009). Sealed tubes (1 mm of thickness, 7 mm of internal diameter and 3 cm of length) with 1.0 ml of bacteriocin solutions, added of powder milk, were placed in a thermostatically controlled dry bath (Accublock Digital Dry Baths, Labnet International In, NJ, USA).…”

Section: Heat Treatmentmentioning

confidence: 99%

“…First-order reaction has been reported to describe heat inactivation of bacteriocins (Lappe et al, 2009), and it is algebraically described for the equation:…”

Section: Estimation Of Kinetic Parametersmentioning

confidence: 99%

Kinetic and thermodynamic study of thermal inactivation of the antimicrobial peptide P34 in milk

2012

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a b s t r a c tThe knowledge on thermal inactivation of biopreservatives in a food matrix is essential to allow their proper utilisation in food industry, enabling the reduction of heating times and optimisation of heating temperatures. In this work, thermal inactivation of the antimicrobial peptide P34 in skimmed and fat milk was kinetically investigated within the temperature range of 90-120°C. The inactivation kinetic follows a first-order reaction with k-values between 0.071 and 0.007 min À1 in skimmed milk, and 0.1346 and 0.0119 min À1 in fat milk. At high temperatures, peptide P34 was less resistant in fat milk, with a significant decrease in residual activity as compared with skimmed milk. At temperatures below 110°C, the fat globules seem to have protective effect to the peptide P34. Results suggest that peptide P34 is heat stable in milk with activation energy of 90 kJ mol À1 in skimmed milk and 136 kJ mol À1 in fat milk.

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“…Half-life is a unit of time and is defined as the time required for loss of half of the original activity [23,24]. The data were fitted to first-order plots and were analyzed as described earlier [25].…”

Section: Storage and Functional Thermostability Analysis Of Endo-inulmentioning

confidence: 99%

Endo-inulinase Stabilization by Pyridoxal Phosphate Modification: A Kinetics, Thermodynamics, and Simulation Approach

Torabizadeh

Habibi-Rezaei

Safari

et al. 2011

Appl Biochem Biotechnol

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The structural and storage and functional thermostabilization of endo-inulinase (EC 3.2.1.7) through semi-rational modification of surface accessible lysine residues by pyridoxal-5'-phosphate (PLP) and ascorbate reduction have been explored. Improved stability was observed on modifications in the absence or presence of inulin, which indicates storage or functional thermostabilization, respectively. Comparisons have been made between non-modified and modified enzyme by the determination of Tm as an indicator of structural stability, temperature-dependent half-lives (t1/2), energy barrier of the inactivation process, and thermodynamic parameters (ΔH, ΔG, and ΔS) in a storage thermostability approach. These parameters coincided well with the observed stabilization of the engineered enzyme. Moreover, relative activities with sucrose and inulin were determined for non-modified and modified endo-inulinases at different temperatures. A comparison of the sucrose-to-inulin ratios of the initial rate of hydrolysis as an indicator of substrate specificity revealed about twofold improvement in inulinase versus sucrose activity by enzyme modification. Molecular dynamics simulations and molecular docking approaches were employed to explain the observed structural and functional thermostabilization of endo-inulinase upon modification. We hypothesize the establishment of intramolecular interactions between the covalently attached PLP-Lys381 and Arg526 and Ser376 residues as a representative of modification-originated intramolecular contacts in the modified enzyme.

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Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A

Cited by 24 publications

References 26 publications

Kinetic and Thermodynamic Analysis of Two Carboxymethylcellulases from Macrotermes subhyalinus Little Soldier

Kinetic and Thermodynamic Analysis of Two Carboxymethylcellulases from Macrotermes subhyalinus Little Soldier

Kinetic and thermodynamic study of thermal inactivation of the antimicrobial peptide P34 in milk

Endo-inulinase Stabilization by Pyridoxal Phosphate Modification: A Kinetics, Thermodynamics, and Simulation Approach

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