Effect of Heat Treatment on Buffalo (Bubalus bubalis) Lactoperoxidase Activity in Raw Milk

Tayefi‐Nasrabadi, Hossein; Asadpour, Reza

doi:10.3923/jbs.2008.1310.1315

Cited by 60 publications

(24 citation statements)

References 1 publication

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“…The fact that higher thermal stability of the immobilized proteins was possibly a consequence of an increase in mutual interaction and protection between the immobilized proteins on the same surface compared with its free form. The z value of the immobilized avidin was lower than that of free avidin (Table 1), which indicated that the immobilized avidin showed more sensitivity to increase in temperature and the free avidin showed more sensitivity to the duration of heat treatment [46].…”

Section: Analysis Of the Ph And Thermal Stability Of Immobilized Avidinmentioning

confidence: 93%

Optimizing immobilization of avidin on surface-modified magnetic nanoparticles: characterization and application of protein-immobilized nanoparticles

Yang

Sun

et al. 2015

Bioprocess Biosyst Eng

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A simple optimization method of immobilization of avidin on magnetic nanoparticles (MNPs)' surface was proposed in this study. The avidin-immobilized MNPs were then developed and used to immobilize a model enzyme [Horseradish peroxidase (HRP)]. The loading capacity (LC) and activity of avidin-immobilized MNPs were optimized through selecting the most appropriate nanoparticle's size and shape, glutaraldehyde concentration, cross-linking reaction time, ultrasonic processing time, and initial concentration of avidin. The LC under optimized conditions was 63.37 ± 1.29 mg avidin/g MNPs, and the immobilized protein was still able to maintain its high biological activity of 10.86 ± 0.13 U/mg (biotin-binding activity of nature avidin was 14.1 U/mg) and better thermal stability compared to free avidin. A highly reusable, stable, and easily recovered immobilized HRP was obtained using MNPs as carriers. The immobilized HRP was reused repeatedly more than 9 times and retained more than 65 % of its original activity.

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Section: Analysis Of the Ph And Thermal Stability Of Immobilized Avidinmentioning

confidence: 93%

Optimizing immobilization of avidin on surface-modified magnetic nanoparticles: characterization and application of protein-immobilized nanoparticles

Yang

Sun

et al. 2015

Bioprocess Biosyst Eng

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“…The activation energy of denaturation of rPPHY is very high as compared to that of the activation energy of catalysis (E a ). The higher value of E d in comparison to E a indicates that a higher amount of energy is required to initiate denaturation as compared to catalysis [41]. Apart from this, activation energy for thermal inactivation (E d ) is higher for rPPHY as compared to that of the wild-type PPHY suggesting that the recombinant phytase exhibits better thermal adaptation than that of wild-type PPHY.…”

Section: Thermal Inactivation Of Rpphymentioning

confidence: 96%

“…The z value of rPPHY, calculated from the slope of graph between log D versus temperature (T°C), is 5.55 Table 4). In general, high z value indicates more sensitivity to the duration of heat treatment, while lower z value indicates high sensitivity to the increase in temperature [41].…”

Section: Thermal Inactivation Of Rpphymentioning

confidence: 97%

Characteristics and Applicability of Phytase of the Yeast Pichia anomala in Synthesizing Haloperoxidase

Joshi

Satyanarayana

2015

Appl Biochem Biotechnol

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The phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids identified by site-directed mutagenesis. Among modulators, N-bromosuccinimide and butanedione inhibit phytase, while Ca(2+) and Ni(2+) stimulate slightly. Vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with phytate. The T 1/2, activation energy (E a ), temperature quotient (Q 10), activation energy of thermal inactivation (Ed), and enthalpy (ΔH d (0) ) of the enzyme are 4.0 min (80 °C), 27.72 kJ mol(-1), 2.1, 410.62 kJ mol(-1), and ∼407.8 kJ mol(-1) (65-80 °C), respectively. The free energy of the process (ΔG d (o) ) increases from 49.56 to 71.58 kJ mol(-1) with rise in temperature, while entropy of inactivation (ΔS d (0) ) remains constant at ∼1.36 kJ mol(-1) K(-1). The supplementation of whole wheat dough with rPPHY resulted in 72.5 % reduction in phytic acid content of bread. These characteristics confirm that the phytase has adequate thermostability for its applicability as a food and feed additive.

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“…4;2017 22 temperatures (Leite et al, 2007). The higher value of Ea means more energy is required to denature the treated enzyme as postulated by Tayefi-Nasrabadi and Asadpour (2008).…”

Section: Thermal Inactivation Kinetics Of Carboxylmethylcellulasesmentioning

confidence: 99%

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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Effect of Heat Treatment on Buffalo (Bubalus bubalis) Lactoperoxidase Activity in Raw Milk

Cited by 60 publications

References 1 publication

Optimizing immobilization of avidin on surface-modified magnetic nanoparticles: characterization and application of protein-immobilized nanoparticles

Optimizing immobilization of avidin on surface-modified magnetic nanoparticles: characterization and application of protein-immobilized nanoparticles

Characteristics and Applicability of Phytase of the Yeast Pichia anomala in Synthesizing Haloperoxidase

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

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