Purification and characterization of a novel glucoamylase from Fusarium solani

Bhatti, Haq Nawaz; Rashid, Mohammad Hamid; Nawaz, Rakhshanda; Asgher, Muhammad; Perveen, Raheela; Jabbar, Abdul

doi:10.1016/j.foodchem.2006.07.058

Cited by 50 publications

(54 citation statements)

References 19 publications

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“…has approximately 1.7, 3.1 and 9-fold lower K m values, respectively which indicates higher affinity of enzyme towards starch. The efficiency constant of glucoamylase was found to be about 1.4 and 2.8 times higher than other reported glucoamylase [1,14] which confirm higher affinity of enzyme towards starch hydrolysis. The enthalpy of activation (DH*), Gibbs free energy (DG*) and entropy of activation (DS*) for starch hydrolysis by glucoamylase were calculated as 23.973, 57.851 and -113.68 J mol -1 , respectively.…”

Section: Kinetics and Thermodynamics Of Starch Hydrolysismentioning

confidence: 45%

“…The efficiency constant (K cat /K m ) was 383.76, indicating high catalytic power of enzyme. The K m values of 1.9, 3.5 and 10 mg ml -1 for starch have been reported for glucoamylases from F. solani [1], A. niger [24] and Acremonium sp. [5].…”

Section: Kinetics and Thermodynamics Of Starch Hydrolysismentioning

confidence: 75%

“…Protein was eluted by applying same buffer and fractions of 1 ml each were collected at flow rate of 0.75 ml min -1 . These fractions were checked for protein concentration at 280 nm and glucoamylase activity [1].…”

Section: Purification Of Glucoamylasementioning

confidence: 99%

“…Many fungal glucoamylases have been reported to be stable at considerably higher temperature for short time periods while glucoamylase produced by Lactobacillus amylovorus was thermolabile and its activity decreased after 10 min exposure at 60°C [25]. The glucoamylase from F. solani was thermally unstable at 60°C and displayed half life of about 26 min [1]. The inactivation constant increases with the temperature, indicating that high temperatures increase the rate of inactivation.…”

Section: Thermostability and Thermodynamics Of The Glucoamylasementioning

confidence: 99%

“…Glucoamylase is second to proteases in worldwide distribution and sales among industrial enzymes. Glucoamylases are widely distributed among many species of animals, plants and microorganisms [1]. Among microbes bacteria, yeast and fungi are capable of producing these enzymes.…”

Section: Introductionmentioning

confidence: 99%

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Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

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Extracellular glucoamylase of Colletotrichum sp. KCP1 produced through solid state fermentation was purified by two steps purification process comprising ammonium sulphate precipitation followed by gel permeation chromatography (GPC). The Recovery of glucoamylase after GPC was 50.40 % with 19.3-fold increase in specific activity. The molecular weight of enzyme was found to be 162.18 kDa by native-PAGE and was dimeric protein of two sub-units with molecular weight of 94.62 and 67.60 kDa as determined by SDS-PAGE. Activation energy for starch hydrolysis was 26.45 kJ mol -1 while temperature quotient (Q 10 ) was found to be 1.9. The enzyme was found to be stable over wide pH range and thermally stable at 40-50°C up to 120 min while exhibited maximum activity at 50°C with pH 5.0. The pKa 1 and pKa 2 of ionisable groups of active site controlling V max were 3.5 and 6.8, respectively. V max , K m and K cat for starch hydrolysis were found to be 58.82 U ml -1 , 1.17 mg (starch) ml -1 and 449 s -1 , respectively. Activation energy for irreversible inactivation (E a(d) ) of glucoamylase was 74.85 kJ mol -1 . Thermodynamic parameters of irreversible inactivation of glucoamylase and starch hydrolysis were also determined.

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Section: Kinetics and Thermodynamics Of Starch Hydrolysismentioning

confidence: 45%

Section: Kinetics and Thermodynamics Of Starch Hydrolysismentioning

confidence: 75%

Section: Purification Of Glucoamylasementioning

confidence: 99%

Section: Thermostability and Thermodynamics Of The Glucoamylasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

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Enhanced Removal of Cu(II) and Pb(II) from Aqueous Solutions by Pretreated Biomass of Fusarium Solani

Bhatti

Samin

Hanif

2008

J Chinese Chemical Soc

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This study investigated the feasibility of Fusarium solani biomass as a biosorbent for Cu(II) and Pb(II) removal from aqueous solutions. Batch sorption experiments were carried out for Cu(II) and Pb(II) to quantify the sorption kinetics, pH, biosorbent dose and pretreatment of F. solani biomass. Biomass metal uptake clearly competed with protons present in the aqueous medium, making pH an important variable in the process. The maximum biosorption by F. solani biomass was obtained with solutions having pH 5 for both metal ions. An enhanced Cu(II) removal (96.53%) was observed for aluminum hydroxide pretreated biomass. Maximum Pb(II) removal (95.48%) was observed with native biomass. Time dependence experiments for the metal ions uptake showed that adsorption equilibrium reached almost 240 min after metal addition. The kinetic studies showed that the biosorption process followed the pseudo secondorder rate model for Cu(II) and Pb(II). The equilibrium data fitted well to the Langmiur isotherm model.

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Kinetic and thermodynamic characterization of lipase from Aspergillus melleus and its biocatalytic performance for degradation of poly(ɛ‐caprolactone)

Amin

Bhatti

Bilal

2021

J of Chemical Tech & Biotech

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BACKGROUND: Lipases are an interesting class of enzymes that can be used as biocatalysts for poly(ɛ-caprolactone) degradation. This work reports on the biochemical characterization of a lipase produced through solid-state fermentation by Aspergillus melleus and its application to degrade poly(ɛ-caprolactone).RESULTS: Lipase demonstrated the best activity and remained stable even after 24 h at an optimal pH of 7.5 and 40 °C. The K m and V max values for p-nitrophenyl palmitate hydrolysis derived from Lineweaver-Burk plot were 0.286 mmol L −1 and 142.86 ∼mol mL −1 min −1 , respectively. Thermal inactivation studies revealed a half-life of 1732.5 min (28.88 h) at 40 °C, and dramatically reduced at elevated temperatures. The activation energy for substrate hydrolysis was 28.81 kJ mol −1 , whereas the entropy, enthalpy (ΔH°) and free energy (ΔG°) of thermal inactivation of lipase were determined to be 168.73 J mol −1 K −1 , 160.60 and 107.79 kJ mol −1 , respectively, at 40 °C. Increase in temperature showed a decline in ΔG°, but ΔH* remained constant. Incubation with organic solvents did not influence the enzyme stability; however, urea and guanidine hydrochloride reduced the lipase activity. Under optimal operating conditions, the enzyme presented excellent biocatalytic ability to poly(ɛ-caprolactone) film degradation, leading to 53% weight loss. Characterization techniques, such as Fourier transform infrared, differential scanning calorimetry and scanning electron microscopy, corroborated the effective biodegradation of poly(ɛ-caprolactone).CONCLUSION: In conclusion, broad working pH, marked stability in the presence of organic solvents, and poly(ɛ-caprolactone) degradation constitutes a lipase from A. melleus as a promising candidate for large-scale bioremediation of solid waste.

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Purification and characterization of a novel glucoamylase from Fusarium solani

Cited by 50 publications

References 19 publications

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Enhanced Removal of Cu(II) and Pb(II) from Aqueous Solutions by Pretreated Biomass of Fusarium Solani

Kinetic and thermodynamic characterization of lipase from Aspergillus melleus and its biocatalytic performance for degradation of poly(ɛ‐caprolactone)

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