Purification and characterization of extracellular phytase from Aspergillus niger ATCC 9142

Casey, A. N. J.; Walsh, Gary

doi:10.1016/s0960-8524(02)00145-1

Cited by 94 publications

(59 citation statements)

References 16 publications

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“…All other compounds tested were only marginally hydrolysed by the purified enzyme. These results are broadly similar to values reported for phytases purified from other A. niger strains (3,6,21,24). The kinetic constants were also in close agreement to those reported for A. niger var.…”

Section: Discussionsupporting

confidence: 89%

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Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

Greiner¹,

Silva

Couri

2009

Braz. J. Microbiol.

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An extracellular phytase from Aspergillus niger 11T53A9 was purified about 51-fold to apparent homogeneity with a recovery of 20.3% referred to the phytase activity in the crude extract. Purification was achieved by ammonium sulphate precipitation, ion chromataography and gel filtration. The purified enzyme behaved as a monomeric protein with a molecular mass of about 85 kDa and exhibited maximal phytate-degrading activity at pH 5.0. Optimum temperature for the degradation of phytate was 55°C. The kinetic parameters for the hydrolysis of sodium phytate were determined to be K M = 54 µmol l -1 and k cat = 190 sec -1 at pH 5.0 and 37°C.The purified enzyme was rather specific for phytate dephosphorylation. It was shown that the phytase preferably dephosphorylates myo-inositol hexakisphosphate in a stereospecific way by sequential removal of phosphate groups via D-Ins(1,2,4,5,6)P 5 , D-Ins(1,2,5,6)P 4 , D-Ins(1,2,6)P 3 , D-Ins(1,2)P 2 to finally Ins(2)P.

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Section: Discussionsupporting

confidence: 89%

“…The pH versus activity profiles of the purified phytase displayed substantial similarity in having two distinct pH optima, an identifying characteristic of the phytaseA enzyme from A. niger (3,25,27). As with the phytase from A. niger var.…”

Section: Discussionmentioning

confidence: 89%

Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

Greiner¹,

Silva

Couri

2009

Braz. J. Microbiol.

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“…The enzyme showed a pH optimum of 5.5 ( Fig. 2A) and more than 80% of the maximal activity was observed at pH values between 4.5-6.5, which closely matches the pH range at potential sites of action, like the salivary glands (pH 5.0) and upper part of the small intestine (pH 4.0-6.0) (Casey and Walsh, 2003 (Yoon et al, 1996) and Aeromonas sp. (Seo et al, 2005) exhibited optimum activity at neutral or alkaline pH of 6.5-8.5.…”

Section: ⅲ Results and Discussionsupporting

confidence: 63%

General Properties of Phytase Produced by Fluorescent Pseudomonas sp. BUN1

Cho¹

2009

Journal of Animal Science and Technology

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)과 같은 금속 2 가이온에 대하여 그 효소활성이 강하게 억제되었다. 또한 BUN1 균주의 효소생산 배지 (PSM) [0.5% sodium phytate, 0.5% (NH4)2SO4, 0.5% KCl, 0.01% MgSO4 ․ 7H2O, 0.01% CaCl2 ․ 2H2O, 0.01% NaCl, 0.001% FeSO4 ․ 7H2O, 0.001% MnSO4 ․ 4H2O; pH 6.5]에 탄소원으로서 옥수수전분 (corn starch)의 첨가는 조사된 다른 탄소 배지원에 비하여 현저하게 파이테이즈 (phytase) 생산을 촉진시켰다.

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“…Gargova et al (1997) on studying 203 fungal strains belonging to the genera Aspergillus, Mucor, Penicillium and Rhizopus, observed clear zones around 91.6% of the colonies. The Aspergillus species, A. oryzae (Chantasartrasamee et al, 2005), A. ficcum (Bogar et al, (Casey and Walsh, 2003;Vassilev et al, 2007;Bhavsar et al, 2012;Bhavsar et al, 2013) were hypothesised to be good phytase producers. The production of phytase by A. japonicus URM 5633 on different agro-industrial substrates was assayed.…”

Section: Resultsmentioning

confidence: 99%

“…Phytases from Aspergillus species usually exhibit optimum temperatures between 50 and 65°C (Vats and Banerjee, 2004). Casey and Walsh (2003) observed increased activity at 65°C and at optimum pH of 5.0 for phytase from A. niger ATCC 9142. However, Escobin-Mopera et al (2012), working with phytase from Klebsiella pneumoniae 9-3B, observed a 15% reduction in enzyme activity at 60°C after only 10 min.…”

Section: Enzyme Characterizationmentioning

confidence: 95%

Optimization of phytase production by Aspergillus japonicus Saito URM 5633 using cassava bast as substrate in solid state fermentation

Moreira¹,

Herculano²,

Maciel³

et al. 2014

Afr. J. Microbiol. Res.

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Production of phytase by Aspergillus japonicus URM 5633 was investigated by solid state fermentation (SSF) using cassava bast as substrate. The effects of temperature, pH and initial moisture on phytase production were studied using a full factorial design 2 3 . The maximum phytase activity was 174 U/g dry substrate. The optimum conditions for phytase production were pH 6.5 and 40% initial moisture at 26°C with 96 h of fermentation. A factorial design 2 2 was created to optimise phytase production, where the initial moisture and temperature were the variables studied. The parameters for phytase production were fixed at 30% initial moisture, 30°C and pH 5.5, and the maximum activity obtained was 183.1 U/g dry substrate. The effects of glucose concentration, nitrogen source type and nitrogen source concentration in phytase production was studied using the 2 3 factorial design. Nitrogen source concentration was significant for phytase activity and had a negative effect, indicating that smaller values increased enzyme activity. The optimum activity for phytase occurred at pH 3.6 and at an apparent optimum temperature of 60°C. Phytase was stable in the pH range of 2.4-3.0 at 30-70°C. The enzymatic activity increased significantly in the presence of FeSO 4 .

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Purification and characterization of extracellular phytase from Aspergillus niger ATCC 9142

Cited by 94 publications

References 16 publications

Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9

General Properties of Phytase Produced by Fluorescent Pseudomonas sp. BUN1

Optimization of phytase production by Aspergillus japonicus Saito URM 5633 using cassava bast as substrate in solid state fermentation

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