scholarly journals Heat inactivation kinetics of Hypocrea orientalis β-glucosidase with enhanced thermal stability by glucose

2015 ◽  
Vol 81 ◽  
pp. 1012-1018 ◽  
Author(s):  
Xin-Qi Xu ◽  
Yan Shi ◽  
Xiao-Bing Wu ◽  
Xi-Lan Zhan ◽  
Han-Tao Zhou ◽  
...  
2021 ◽  
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.


1999 ◽  
Vol 65 (12) ◽  
pp. 5364-5371 ◽  
Author(s):  
Patrick C. Wouters ◽  
Nicole Dutreux ◽  
Jan P. P. M. Smelt ◽  
Huub L. M. Lelieveld

ABSTRACT The effects of pulsed electric field (PEF) treatment and processing factors on the inactivation kinetics of Listeria innocuaNCTC 11289 were investigated by using a pilot plant PEF unit with a flow rate of 200 liters/h. The electric field strength, pulse length, number of pulses, and inlet temperature were the most significant process factors influencing the inactivation kinetics. Product factors (pH and conductivity) also influenced the inactivation kinetics. In phosphate buffer at pH 4.0 and 0.5 S/m at 40°C, a 3.0-V/μm PEF treatment at an inlet temperature of 40°C resulted in ≥6.3 log inactivation of strain NCTC 11289 at 49.5°C. A synergistic effect between temperature and PEF inactivation was also observed. The inactivation obtained with PEF was compared to the inactivation obtained with heat. We found that heat inactivation was less effective than PEF inactivation under similar time and temperature conditions.L. innocua cells which were incubated for a prolonged time in the stationary phase were more resistant to the PEF treatment, indicating that the physiological state of the microorganism plays a role in inactivation by PEF. Sublethal injury of cells was observed after PEF treatment, and the injury was more severe when the level of treatment was increased. Overall, our results indicate that it may be possible to use PEF in future applications in order to produce safe products.


1976 ◽  
Vol 22 (3) ◽  
pp. 359-363 ◽  
Author(s):  
G. Molin ◽  
K. Östlund

The dry-heat inactivation kinetics of Bacillus subtilis var. niger (ATCC 9372) spores has been studied in the temperature range of 120–190 °C. The spores were applied to glass plates of a standardized area (3.24 cm2).Spore preparations of five different spore densities were used (8.3 × 104, 7.4 × 105, 7.8 × 106, 6.3 × 107, and 6.6 × 108 spores per sample, respectively). The heat resistance of the spore was dependent on the number of spores per surface unit. Maximum resistance was observed when the concentration was 7.4 × 105 spores per sample. The D-values obtained at 160 °C from these samples were about twice as high as the D-values obtained from samples with a concentration of 6.3 × 107 or 6.6 × 108 spores per sample. The z value was found to be independent of spore density. Thus, for the two concentrations 7.4 × 105 and 6.3 × 107 spores per sample, the z-value was found to be 22 °C and constant over the temperature range investigated.


2012 ◽  
Vol 95 (1) ◽  
pp. 20-35 ◽  
Author(s):  
L.E. Pearce ◽  
B.W. Smythe ◽  
R.A. Crawford ◽  
E. Oakley ◽  
S.C. Hathaway ◽  
...  

Genetics ◽  
1978 ◽  
Vol 90 (4) ◽  
pp. 725-734
Author(s):  
Susan A Meredith ◽  
Roger E Ganschow

ABSTRACT A difference in the heat-inactivation kinetics between the β-glucuronidases of C3HeB/FeJ and C57Bl/6J mice was utilized to assess the mode of action of a temporal genetic element in controlling the expression of the β-glucuronidase structural gene Gus. The heat-inactivation kinetics of liver and kidney β-glucuronidase from F1 C3HeB/FeJ x C57Bl/6J animals were intermediate with respect to the parental enzyme patterns, suggesting that equal concentrations of the two allelic products were present in β-glucuronidase tetramers of F1 progeny. β-glucuronidase heteropolymers assembled in vivo under conditions where equal concentrations of the two structural alleles of the enzyme were known to be present also exhibited intermediate heat-inactivation kinetics. These observations are consistent with a trans mode of action of a genetic element that controls the rate of murine β-glucuronidase synthesis.


1970 ◽  
Vol 20 (4) ◽  
pp. 573-578 ◽  
Author(s):  
W. W. Bond ◽  
M. S. Favero ◽  
N. J. Petersen ◽  
J. H. Marshall

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.


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.


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