scholarly journals Peroxidase isoenzymes from seedlings of VIGNA sp (V) landrace Vn: distribution and thermal stability

Author(s):  
Yves Mann Elate Lea Mbassi ◽  
Marie Solange Evehe Bebandoue ◽  
Wilfred Fon Mbacham

Abstract Several soluble peroxidase isoenzymes are expressed in a landrace of Vigna sp cultivated in the north of Cameroon (landrace called Vn in previous study) during seed germination. There are at least two cathodic peroxidases and eight major anodic peroxidases as shown by their electrophoretic migration at pH 7.4 under native conditions. These isoperoxidases are more expressed in radicles than in shoots. They have different thermal stability, so that heat inactivation kinetics of crude peroxidase extracts from radicles does not fit the first-order model. One major anodic isoperoxidase of the slow migrating group and at least two others anodic isoperoxidases of the The slow and intermediate migrating groups of anodic isoperoxidasesanodic isoperoxidases are stable for ten minutes of incubation at 80°C and 85°C. The major anodic isoperoxidase of the The less anodic slow migrating groupisoperoxidase (named A6 in this study) shows in addition to this great thermal stability, a high activity during germination and is expressed both in radicles and shoots in large amounts. The combination of those characteristics makes thisthat isoperoxidase a a potential candidate for biotechnological applications.

2021 ◽  
Vol 12 (3) ◽  
pp. 476-483
Author(s):  
Yves Mann Elate Lea Mbassi ◽  
Marie Solange Evehe ◽  
Wilfred Fon Mbacham ◽  
John Payne Muluh

Several soluble peroxidase isoenzymes are expressed in a landrace of Vigna sp. cultivated in the north of Cameroon (landrace called Vn in previous study) during seed germination. There are at least two cathodic peroxidases and eight major anodic peroxidases as shown by their electrophoretic migration at pH 7.4 under native conditions. These isoperoxidases are more expressed in roots than in shoots. They have different thermal stability, so that heat inactivation kinetics of crude peroxidase extracts from roots do not fit the first-order model. The slow and intermediate migrating groups of anodic isoperoxidases retains a substantial activity after ten minutes of incubation at 80°C and 85°C. An anodic isoperoxidase (named A6 in this study) shows in addition to this great thermal stability, a high activity in seedlings and is expressed both in roots and shoots. The combination of those characteristics makes this isoperoxidase a potential candidate for biotechnological applications. Three major anodic isoperoxidases, of which A6 and another thermostable isoperoxidase, were successfully separated from each other by ion exchange chromatography on DEAE-cellulose, after precipitation of total proteins by ice-cold acetone. This offers the prospect of being able to characterize these isoperoxidases individually in future studies.


2016 ◽  
Vol 79 (9) ◽  
pp. 1482-1489
Author(s):  
HAYRIYE BOZKURT ◽  
JAIRUS R. D. DAVID ◽  
RYAN J. TALLEY ◽  
D. SCOTT LINEBACK ◽  
P. MICHAEL DAVIDSON

ABSTRACT Sporolactobacillus species have been occasionally isolated from spoiled foods and environmental sources. Thus, food processors should be aware of their potential presence and characteristics. In this study, the heat resistance and influence of the growth and recovery media on apparent heat resistance of Sporolactobacillus nakayamae spores were studied and described mathematically. For each medium, survivor curves and thermal death curves were generated for different treatment times (0 to 25 min) at different temperatures (70, 75, and 80°C) and Weibull and first-order models were compared. Thermal inactivation data for S. nakayamae spores varied widely depending on the media formulations used, with glucose yeast peptone consistently yielding the highest D-values for the three temperatures tested. For this same medium, the D-values ranged from 25.24 ± 1.57 to 3.45 ± 0.27 min for the first-order model and from 24.18 ± 0.62 to 3.50 ± 0.24 min for the Weibull model at 70 and 80°C, respectively. The z-values determined for S. nakayamae spores were 11.91 ± 0.29°C for the Weibull model and 11.58 ± 0.43°C for the first-order model. The calculated activation energy was 200.5 ± 7.3 kJ/mol for the first-order model and 192.8 ± 22.1 kJ/mol for the Weibull model. The Weibull model consistently produced the best fit for all the survival curves. This study provides novel and precise information on thermal inactivation kinetics of S. nakayamae spores that will enable reliable thermal process calculations for eliminating this spoilage bacterium.


2015 ◽  
Vol 81 (14) ◽  
pp. 4850-4859 ◽  
Author(s):  
Hayriye Bozkurt ◽  
Doris H. D'Souza ◽  
P. Michael Davidson

ABSTRACTHuman noroviruses (HNoV) and hepatitis A virus (HAV) have been implicated in outbreaks linked to the consumption of presliced ready-to-eat deli meats. The objectives of this research were to determine the thermal inactivation kinetics of HNoV surrogates (murine norovirus 1 [MNV-1] and feline calicivirus strain F9 [FCV-F9]) and HAV in turkey deli meat, compare first-order and Weibull models to describe the data, and calculate Arrhenius activation energy values for each model. TheD(decimal reduction time) values in the temperature range of 50 to 72°C calculated from the first-order model were 0.1 ± 0.0 to 9.9 ± 3.9 min for FCV-F9, 0.2 ± 0.0 to 21.0 ± 0.8 min for MNV-1, and 1.0 ± 0.1 to 42.0 ± 5.6 min for HAV. Using the Weibull model, thetD = 1(time to destroy 1 log) values for FCV-F9, MNV-1, and HAV at the same temperatures ranged from 0.1 ± 0.0 to 11.9 ± 5.1 min, from 0.3 ± 0.1 to 17.8 ± 1.8 min, and from 0.6 ± 0.3 to 25.9 ± 3.7 min, respectively. Thez(thermal resistance) values for FCV-F9, MNV-1, and HAV were 11.3 ± 2.1°C, 11.0 ± 1.6°C, and 13.4 ± 2.6°C, respectively, using the Weibull model. Thezvalues using the first-order model were 11.9 ± 1.0°C, 10.9 ± 1.3°C, and 12.8 ± 1.7°C for FCV-F9, MNV-1, and HAV, respectively. For the Weibull model, estimated activation energies for FCV-F9, MNV-1, and HAV were 214 ± 28, 242 ± 36, and 154 ± 19 kJ/mole, respectively, while the calculated activation energies for the first-order model were 181 ± 16, 196 ± 5, and 167 ± 9 kJ/mole, respectively. Precise information on the thermal inactivation of HNoV surrogates and HAV in turkey deli meat was generated. This provided calculations of parameters for more-reliable thermal processes to inactivate viruses in contaminated presliced ready-to-eat deli meats and thus to reduce the risk of foodborne illness outbreaks.


1999 ◽  
Vol 62 (10) ◽  
pp. 1215-1217 ◽  
Author(s):  
A. LÓPEZ-MALO ◽  
S. GUERRERO ◽  
S. M. ALZAMORA

Inactivation kinetics of Saccharomyces cerevisiae during thermal treatments at moderate temperatures (45.0, 47.5, 50.0, 52.5, or 55.0°C) combined with application of 20 kHz of ultrasound were evaluated. S. cerevisiae inactivation under the combined effects of heat and ultrasound followed first-order reaction kinetics, with decimal reduction times (D) that varied from 22.3 to 0.8 min. D values in treatments that combined heat and ultrasound were significantly smaller (P < 0.05) than D values obtained for thermal treatments and were more noticeable at temperatures below 50°C. The dependence of the D value on temperature had a significantly (P < 0.05) greater z value for combined treatments. Yeast heat inactivation kinetics revealed decreased thermal resistance caused by ultrasound.


2015 ◽  
Vol 81 ◽  
pp. 1012-1018 ◽  
Author(s):  
Xin-Qi Xu ◽  
Yan Shi ◽  
Xiao-Bing Wu ◽  
Xi-Lan Zhan ◽  
Han-Tao Zhou ◽  
...  

2013 ◽  
Vol 76 (1) ◽  
pp. 79-84 ◽  
Author(s):  
HAYRIYE BOZKURT ◽  
DORIS H. D'SOUZA ◽  
P. MICHAEL DAVIDSON

Studies are needed to bridge existing data gaps and determine appropriate parameters for thermal inactivation methods for human noroviruses. Cultivable surrogates, such as feline calicivirus (FCV-F9) and murine norovirus (MNV-1), have been used in the absence of human norovirus infectivity assays. This study aimed to characterize the thermal inactivation kinetics of MNV-1 and FCV-F9 at 50, 56, 60, 65, and 72°C for different treatment times (0 to 60 min). Thermal inactivation was performed using the capillary tube method with titers of 4.0 × 107 (MNV-1) and 5.8 × 108 (FCV-F9) PFU/ml in triplicate experiments, followed by standard plaque assays in duplicate for each experiment. Weibull and first-order models were compared to describe survival curve kinetics. Model fitness was investigated by comparing the regression coefficients (R2) and the chi-square (χ2) and root mean square error (RMSE) values. The D-values calculated from the first-order model (50 to 72°C) were 0.15 to 34.49 min for MNV-1 and 0.11 to 20.23 min for FCV-9. Using the Weibull model, the tD values needed to destroy 1 log PFU of MNV-1 and FCV-F9 at the same temperatures were 0.11 to 28.26 and 0.06 to 13.86 min, respectively. In terms of thermal resistance, MNV-1 was more sensitive than FCV-F9 up to 65°C. At 72°C, FCV-F9 was slightly more susceptible to heat inactivation. Results revealed that the Weibull model was more appropriate to represent the thermal inactivation behavior of both tested surrogates. The z-values were calculated using D-values for the first-order model and the tD values for the Weibull model. The z-values were 9.31 and 9.19°C for MNV-1 and 9.36 and 9.31°C for FCV-F9 for the first-order and Weibull models, respectively. This study provides more precise information than previous reports on the thermal inactivation kinetics of two norovirus surrogates for use in thermal process calculations.


Materials ◽  
2021 ◽  
Vol 14 (11) ◽  
pp. 2872
Author(s):  
Seyed Mohamad Reza Paran ◽  
Ghasem Naderi ◽  
Elnaz Movahedifar ◽  
Maryam Jouyandeh ◽  
Krzysztof Formela ◽  
...  

The effect of several concentrations of carboxylated nitrile butadiene rubber (XNBR) functionalized halloysite nanotubes (XHNTs) on the vulcanization and degradation kinetics of XNBR/epoxy compounds were evaluated using experimental and theoretical methods. The isothermal vulcanization kinetics were studied at various temperatures by rheometry and differential scanning calorimetry (DSC). The results obtained indicated that the nth order model could not accurately predict the curing performance. However, the autocatalytic approach can be used to estimate the vulcanization reaction mechanism of XNBR/epoxy/XHNTs nanocomposites. The kinetic parameters related to the degradation of XNBR/epoxy/XHNTs nanocomposites were also assessed using thermogravimetric analysis (TGA). TGA measurements suggested that the grafted nanotubes strongly enhanced the thermal stability of the nanocomposite.


2017 ◽  
Vol 23 (4) ◽  
pp. 495-506 ◽  
Author(s):  
Larissa Falleiros ◽  
Bruna Cabral ◽  
Janaína Fischer ◽  
Carla Guidini ◽  
Vicelma Cardoso ◽  
...  

The immobilization and stabilization of Aspergillus oryzae ?-galactosidase on Duolite??A568 was achieved using a combination of physical adsorption, incubation step in buffer at pH 9.0 and cross-linking with glutaraldehyde and in this sequence promoted a 44% increase in enzymatic activity as compared with the biocatalyst obtained after a two-step immobilization process (adsorption and cross-linking). The stability of the biocatalyst obtained by three-step immobilization process (adsorption, incubation in buffer at pH 9.0 and cross-linking) was higher than that obtained by two-steps (adsorption and cross-linking) and for free enzyme in relation to pH, storage and reusability. The immobilized biocatalyst was characterized with respect to thermal stability in the range 55-65 ?C. The kinetics of thermal deactivation was well described by the first-order model, which resulted in the immobilized biocatalyst activation energy of thermal deactivation of 71.03 kcal/mol and 5.48 h half-life at 55.0 ?C.


2014 ◽  
Vol 77 (2) ◽  
pp. 276-283 ◽  
Author(s):  
HAYRIYE BOZKURT ◽  
DORIS H. D'SOUZA ◽  
P. MICHAEL DAVIDSON

Leafy greens, including spinach, have potential for human norovirus transmission through improper handling and/or contact with contaminated water. Inactivation of norovirus prior to consumption is essential to protect public health. Because of the inability to propagate human noroviruses in vitro, murine norovirus (MNV-1) and feline calicivirus (FCV-F9) have been used as surrogates to model human norovirus behavior under laboratory conditions. The objectives of this study were to determine thermal inactivation kinetics of MNV-1 and FCV-F9 in spinach, compare first-order and Weibull models, and measure the uncertainty associated with the process. D-values were determined for viruses at 50, 56, 60, 65, and 72°C in 2-ml vials. The D-values calculated from the first-order model (50 to 72°C) ranged from 0.16 to 14.57 min for MNV-1 and 0.15 to 17.39 min for FCV-9. Using the Weibull model, the tD for MNV-1 and FCV-F9 to destroy 1 log (D = 1) at the same temperatures ranged from 0.22 to 15.26 and 0.27 to 20.71 min, respectively. The z-values determined for MNV-1 were 11.66 ± 0.42°C using the Weibull model and 10.98 ± 0.58°C for the first-order model and for FCV-F9 were 10.85 ± 0.67°C and 9.89 ± 0.79°C, respectively. There was no difference in D- or z-value using the two models (P >0.05). Relative uncertainty for dilution factor, personal counting, and test volume were 0.005, 0.0004, and ca. 0.84%, respectively. The major contribution to total uncertainty was from the model selected. Total uncertainties for FCV-F9 for the Weibull and first-order models were 3.53 to 7.56% and 11.99 to 21.01%, respectively, and for MNV-1, 3.10 to 7.01% and 13.14 to 16.94%, respectively. Novel and precise information on thermal inactivation of human norovirus surrogates in spinach was generated, enabling more reliable thermal process calculations to control noroviruses. The results of this study may be useful to the frozen food industry in designing blanching processes for spinach to inactivate or control noroviruses.


2019 ◽  
Vol 44 (4) ◽  
pp. 307-315 ◽  
Author(s):  
Xueya Dai ◽  
Hua Song ◽  
Hualin Song ◽  
Jing Gong ◽  
Feng Li ◽  
...  

A nickel phosphide hydrodeoxygenation catalyst (Ni2P-O/MCM-41) was prepared using a new synthetic method. The as-prepared catalyst was evaluated in the hydrodeoxygenation of benzofuran, and the effects of reaction temperature, pressure, and the H2/liquid ratio were investigated. A pseudo first-order model was employed to describe the reaction kinetics of benzofuran hydrodeoxygenation over the Ni2P-O/MCM-41 catalyst. The reaction rate constants ( k1– k5) at different temperatures were determined according to this model. At 533 K, the conversion of 2-ethylphenol in to ethylbenzene began to increase dramatically, and the yield of O-free product, ethylcyclohexane, started to increase rapidly. At 573 K, 3.0 MPa, and a H2/liquid ratio of 500 (V/V), the conversion of benzofuran over Ni2P-O/MCM-41 reached 93%, and the combined yield of O-free products was 91%. Contact time analysis indicated that demethylation was not favored over the Ni2P-O/MCM-41 catalyst.


Sign in / Sign up

Export Citation Format

Share Document