Thermostability of crude endoglucanase from Aspergillus fumigatus grown under solid state fermentation (SSF) and submerged fermentation (SmF)

Saqib, Abdul Aala Najmus; Hassan, Madiha; Khan, Nahida Farooq; Baig, Shahjahan

doi:10.1016/j.procbio.2009.12.011

Cited by 124 publications

(81 citation statements)

References 37 publications

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“…This is due to the negative entropic contribution during the process (Tanaka and Hoshino, 2002;Pal and Khanum, 2011). The values obtained here are close to the ones obtained from crude endoglucanase from Aspergillus fumigatus grown under submerged fermentation (Saqib et al, 2010). This is an indication that the two enzymes may have similar amino acid sequence.…”

Section: Table I Summary Of the Thermoinactivation And Thermodynamicsupporting

confidence: 84%

“…The denaturation process proceeds through an unstable intermediate transition (or activated) state, U (Siddiqui et al, 1997). As long as the initial input of energy is less than the Ea (D) the unstable intermediate (U) can fold back into the native state (N) upon cooling (Saqib et al, 2010). This activation barrier is crucial to the stability and survival of the biomolecules in nature.…”

Section: Table I Summary Of the Thermoinactivation And Thermodynamicmentioning

confidence: 99%

See 1 more Smart Citation

Thermostability and thermodynamic characterization of sprouted pearl millet ?-amylases for its biotechnological applications

Agbo

Okwuenu

Ezugwu

et al. 2017

Bangladesh J. Sci. Ind. Res.

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There is an increasing demand for amylolytic products such as glucose syrup in biotechnological industries. Starch liquification by α-amylase must take place at temperatures higher than the gelatinization temperatures and the use for thermostable α-amylase is therefore required. Two (or) isotypes namely amy-1 and amy-2 of α-amylase from pearl millet have been investigated for their thermostability and thermodynamic characterization.Thermal inactivation of α-amylase follows first order kinetics which varies with time and product during inactivation process. The half-life of α-1 was 198 mins at 50ºC. The Ea (inact) was calculated using Arrhenius plot gave 22.00 KCalmol K -1 at 50ºC. This suggest that the α-1 and α-2 are thermostable.

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Section: Table I Summary Of the Thermoinactivation And Thermodynamicsupporting

confidence: 84%

Section: Table I Summary Of the Thermoinactivation And Thermodynamicmentioning

confidence: 99%

Thermostability and thermodynamic characterization of sprouted pearl millet ?-amylases for its biotechnological applications

Agbo

Okwuenu

Ezugwu

et al. 2017

Bangladesh J. Sci. Ind. Res.

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“…In terms of thermal stability, the more reliable parameter to evaluate is Gibbs free energy (ΔG°). 29 Negative or lower values indicate that the reaction favors thermal denaturation. The values encountered in this work confirming high enzyme stability.…”

Section: Thermal Inactivationmentioning

confidence: 99%

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

Feltrin¹,

Fontes²,

Gracia³

et al. 2017

Quim. Nova

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This study established the conditions for the extraction of the enzyme peroxidase (PO) from soybean meal (SBM). An experimental design methodology was carried out in order to evaluate the effects of stirring rate time, pH and extracting solvent volume on the enzyme extraction. By using 5 g SBM and 50 mL phosphate buffer 10 mmol L -1 pH 4.7, 60 min stirring rate at 100 rpm, an enzyme with specific activity of 100 U mg -1 for SBM was obtained. Two techniques of purification were tested and compared for purification of peroxidase from soybean meal: triphasic partition (TPP) and molecular exclusion chromatography. TPP showcased a greater efficiency with 50% recuperation and a purification factor of 13.6. Peroxidase in crude and pure forms was characterized for kinetics, thermodynamics and biochemistry. The parameter of thermal inactivation indicates high stability to exposure time and temperature increase, showing that enzyme activity is not altered by the presence of constituents of the reaction medium. Peroxidase in crude form represented a greater upkeep in activity, keeping 50% activity for 114 days at 0 °C. Peroxidase in pure form had greater affinity for substrate and reduced Deoxynivalenol levels by 80%, 20% more than the crude form.

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“…The enzyme undergoes a first order kinetics reaction, which is responsible for its irreversible denaturation and is expressed in terms of its half life (t1/2). The activation energy and change in Gibbs free energy, enthalpy and entropy between the folded and unfolded states of enzyme are to describe denaturation thermodynamics (Saqib et al, 2010). The activity and thermostability of enzymes are important parameters to determine the economic feasibility in industrial processes.…”

Section: Introductionmentioning

confidence: 99%

POULTRY DROPPING BASED BIODIGESTED SLURRY FOR PROTEASE PRODUCTION BY Humicola fuscoatra MTCC 1409: OPTIMIZATION AND KINETIC STUDY

Goyal¹,

Dar²,

Phutela³

2018

JEBAS

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Protease is one of the most important groups of commercially produced enzymes. This study was aimed at the optimization and kinetics of protease production from poultry dropping based biodigested slurry by Humicola fuscoatra MTCC 1409. Four significant variables (pH, temperature, slurry concentration and inoculum concentration) were considered for optimization both by one variable at a time approach and response surface methodology. The maximum protease production in the poultry dropping based biodigested slurry was (531±1.37 U g -1 ) under the optimum conditions of pH (5), temperature (40°C), slurry concentration (25%) and inoculum concentration (10%). The protease production was found to be 3.38 fold higher under optimized conditions as compared to the non-optimized ones. The thermal inactivation of protease produced from biodigested slurry was investigated kinetically within temperature range of 30-70°C. The irreversible inactivation was well described by first order kinetics with k values increasing between 0.0028 to 0.0071 min -1 and t1/2 decreasing from247.70 to 98.10 mins.At higher temperature, there was significant decrease in residual activity. The activation energy, enthalpy, Gibbs free energy and entropy range calculated on the basis of residual activity experiments conducted at temperature range of 30-70°C was found to be 21.29, 18.44 to 18.78 kJ mol -1

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Thermostability of crude endoglucanase from Aspergillus fumigatus grown under solid state fermentation (SSF) and submerged fermentation (SmF)

Cited by 124 publications

References 37 publications

Thermostability and thermodynamic characterization of sprouted pearl millet ?-amylases for its biotechnological applications

Thermostability and thermodynamic characterization of sprouted pearl millet ?-amylases for its biotechnological applications

Peroxidase from soybean meal: obtention, purification and application in reduction of deoxynivalenol levels

POULTRY DROPPING BASED BIODIGESTED SLURRY FOR PROTEASE PRODUCTION BY Humicola fuscoatra MTCC 1409: OPTIMIZATION AND KINETIC STUDY

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