Studies on Kinetics and Thermostability of a Novel Acid Invertase from<i>Fusarium</i><i>solani</i>

Bhatti, Haq Nawaz; Asgher, Muhammad; Abbas, Ahmed M.; Nawaz, Rakhshanda; Sheikh, Munir A.

doi:10.1021/jf053194g

Cited by 83 publications

(78 citation statements)

References 32 publications

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“…This temperature optimum was higher than that reported for the enzyme from Bifidobacterium infantis ATCC 15697 (Warchol et al 2002), Lactobacillus reuteri (Ginés et al 2000), Fusarium solani (Bhatti et al 2006), Aspergillus niger IMI303386 (Nguyen et al 2005) and A. oryzae KB (Kurakake et al 2008), and similar with that of the β-fructofuranosidases from Aspergillus niger ATCC 20611 and Aureobasidium sp. ATCC 20524 (Yoshikawa et al 2007).…”

Section: Influence Of Temperature and Phmentioning

confidence: 43%

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

Rustiguel¹,

Oliveira²,

Terenzi³

et al. 2011

Electro Journal of Biotech

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The filamentous fungus A. phoenicis produced high levels of β-D-fructofuranosidase (FFase) when grown for 72 hrs under Solid-State Fermentation (SSF), using soy bran moistened with tap water (1:0.5 w/v) as substrate/carbon source. Two isoforms (I and II) were obtained, and FFase II was purified 18-fold to apparent homogeneity with 14% recovery. The native molecular mass of the glycoprotein (12% of carbohydrate content) was 158.5 kDa with two subunits of 85 kDa estimated by SDS-PAGE. Optima of temperature and pH were 55ºC and 4.5. The enzyme was stable for more than 1 hr at 50ºC and was also stable in a pH range from 7.0 to 8.0. FFase II retained 80% of activity after storage at 4ºC by 200 hrs. Dichroism analysis showed the presence of random and β-sheet structure. A. phoenicis

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Section: Influence Of Temperature and Phmentioning

confidence: 43%

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

Rustiguel¹,

Oliveira²,

Terenzi³

et al. 2011

Electro Journal of Biotech

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“…Like pH, temperature stability of enzyme is important for industrial application [27]. The effect of temperature on polygalacturonase production by strain HD2 was studied at different temperature ranging from 30°C to 70°C.…”

Section: Effect Of Ph and Temperature On Enzyme Activitymentioning

confidence: 99%

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Paudel¹,

Lin²,

Shen³

et al. 2015

Microbiol Discov

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Background: Polygalacturonase is an important pectin degrading enzyme. The western honey bee (Apis mellifera L.) collects pollens from different flowers which are rich source of pectin. The microbiota in the gut of honey bee, release polygalacturonase enzyme and help in pectin digestion. This study aims to isolate and characterize novel polygalacturonase producing bacterial strain from honey bee's gut. Methods: The bacterial strain was isolated by using pectin agar plate assay. The bacterial strain was identified on the basis of morphology and 16S rDNA sequence analysis. The enzyme assay was performed by using pectin as a substrate. Biomass of different fruits/vegetables was also used as a source of carbon during fermentation. The protein gel was run using SDS-PAGE for molecular weight determination of the polygalacturonase. Results:The bacterial strain showed the maximum growth, protein and polygalacturonase production at 72 hours of incubation. This bacterial strain was identified as new Bacillus sp. HD2. The sequence of this strain was successfully uploaded in NCBI Genbank database (Accession no. KP676929). The exo polygalacturonase produced by this strain of Bacillus was optimal at 40°C and exhibited enzyme activity in a wide range of pH from pH 5-12. The polygalacturonase production was enhanced by using yeast extract (3%) in the production medium and the enzyme activity was stimulated by Ca 2+ (2 mM) and SDS (200 mM). Biomass of apple's peel (1%) was found as an excellent source of carbon for the polygalacturonase production in fermentation medium (17.11±0.46 μmol ml

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“…Thermostability is the ability of enzyme to resist against thermal unfolding in the absence of substrates [28]. The thermostability of the purified exo-polygalacturonase was determined by measuring the residual activity of the enzyme after incubation at various temperatures ranging from 25 to 65 • C for 10, 20, 30 and 60 min.…”

Section: Effect Of Temperature On Exo-polygalacturonase Activity and mentioning

confidence: 99%

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

Dogan¹,

Tarı²

2008

Biochemical Engineering Journal

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Exo-polygalacturonase enzyme produced by Aspergillus sojae ATCC 20235 was purified using three-phase partitioning (TPP), an emerging bio-separation technique where a single step as compared to the classical multi-step purification was used. Using this technique, crude enzyme solution (pH 6.6) saturated to 30% (w/v) with ammonium sulphate and with a crude extract to tert-butanol ratio of 1:1 (v/v) at 25• C resulted in 25.5% recovery of exo-polygalacturonase with a 6.7-fold purification. The purified enzyme was characterized with respect to its activity and stability at various pH and temperature ranges. Optimum pH and temperature for maximum activity were determined as pH 4 and 55• C. The enzyme was stable at both acidic and alkaline pH for 2 h at 30• C. The thermal stability study showed that the purified enzyme had an inactivation energy of 68.41 kcal/mol and a half-life (t 1/2 ) value of 3.6 h at 75• C presenting a large thermal stability. The kinetic constants K m and V max using polygalacturonic acid as substrate were 0.75 g l −1 and 1.14 mol min −1 , respectively. SDS-PAGE profiling revealed that the purified exopolygalacturonase had two bands with the molecular weights of 36 and 53 kDa. The enzyme was completely inhibited in the presence of Mn 2+ and SDS and induced significantly by EDTA, glycerol and ␤-mercaptoethanol.

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Studies on Kinetics and Thermostability of a Novel Acid Invertase fromFusariumsolani

Cited by 83 publications

References 32 publications

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

Biochemical properties of an extracellular β-D-fructofuranosidase II produced by Aspergillus phoenicis under Solid-Sate Fermentation using soy bran as substrate

Characterization of pectin depolymerising exo polygalacturonase by Bacillus sp. HD2 isolated from the gut of Apis mellifera L.

Characterization of three-phase partitioned exo-polygalacturonase from Aspergillus sojae with unique properties

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