Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

Tran, Thuy Thi; Hashim, Suhaila; Gaber, Yasser; Mamo, Gashaw; Mattìasson, Bo; Hatti‐Kaul, Rajni

doi:10.1016/j.jinorgbio.2011.04.005

Cited by 29 publications

(14 citation statements)

References 29 publications

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“…MD2, had molecular weight in the range of 43–48 kDa. The enzyme showed optimum activity at pH 6.5, which is in the opimum pH range (5.0–8.0) of phytases reported from other Bacillus species . The optimum temperature of B. aryabhattai RS1 phytase was 40°C as reported earlier for phytase from Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

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A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

Roy

Datta

Ghosh

2017

Biotechnology Progress

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Bacillus aryabhattai RS1 isolated from rhizosphere produced an extracellular, low temperature active phytase. The cultural conditions for enzyme production were optimized to obtain 35 U mL of activity. Purified phytase had specific activity and molecular weight of 72.97 U mg and ∼40 kDa, respectively. The enzyme was optimally active at pH 6.5 and 40°C and was highly specific to phytate. It exhibited higher catalytic activity at low temperature, retaining over 40% activity at 10°C. Phytase was more thermostable in presence of Ca ion and retained 100% residual activity on preincubation at 20-50°C for 30 min. Partial phytase encoding gene, phy (816 bp) was cloned and sequenced. The encoded amino acid sequence (272 aa) contained two conserved motifs, DA[A/T/E]DDPA[I/L/V]W and NN[V/I]D[I/L/V]R[Y/D/Q] of β-propellar phytase and had lower sequence homology with other Bacillus phytases, indicating its novelty. Phytase and the bacterial inoculum were effective in improving germination and growth of chickpea seedlings under phosphate limiting condition. Moreover, the potential applications of the enzyme with relatively high activity at lower temperatures (20-30°C) could also be extended to aquaculture and food processing. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:633-641, 2017.

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Section: Discussionmentioning

confidence: 99%

“…KHU-10. 30 The 32 had molecular weight in the range of 43-48 kDa. The enzyme showed optimum activity at pH 6.5, which is in the opimum pH range (5.0-8.0) of phytases reported from other Bacillus species.…”

Section: Discussionmentioning

confidence: 99%

A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

Roy

Datta

Ghosh

2017

Biotechnology Progress

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“…The enzyme was strongly inhibited by EDTA (Figure 7), as previously described (Kerovuo et al, 2000), suggesting that it may be a metalloenzyme. Indeed, Bacillus phytases are catalytically active only when they are structurally associated with Ca 2+ (Oh et al, 2001; Tran et al, 2011; Zeng et al, 2011). On the other hand, the activity of Aspergillus niger van Teighem phytase is enhanced up to about 50% by EDTA (Vats and Banerjee, 2005).…”

Section: Resultsmentioning

confidence: 99%

Degradation of Phytate Pentamagnesium Salt by Bacillus sp. T4 Phytase as a Potential Eco-friendly Feed Additive

Park¹,

Lee²,

Cho³

2012

Asian Australas. J. Anim. Sci

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A bacterial isolate derived from soil samples near a cattle farm was found to display extracellular phytase activity. Based on 16S rRNA sequence analysis, the strain was named Bacillus sp. T4. The optimum temperature for the phytase activity toward magnesium phytate (Mg-InsP6) was 40°C without 5 mM Ca2+ and 50°C with 5 mM Ca2+. T4 phytase had a characteristic bi-hump two pH optima of 6.0 to 6.5 and 7.4 for Mg-InsP6. The enzyme showed higher specificity for Mg-InsP6 than sodium phytate (Na-InsP6). Its activity was fairly inhibited by EDTA, Cu2+, Mn2+, Co2+, Ba2+ and Zn2+. T4 phytase may have great potential for use as an eco-friendly feed additive to enhance the nutritive quality of phytate and reduce phosphorus pollution.

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“…Whereas phytase activity from Bacillus is metal ion dependent as the enzyme needed calcium for activity and stability (Fu et al, 2008). Tran et al (2011) reported that both enzyme stability and activity of a recombinant alkaline phytase obtained from Bacillus sp. MD2 is affected by divalent metal ions (Ca 2C ).…”

Section: Biochemical Characterization and Purification Of Phytasesmentioning

confidence: 99%

Microbial production of phytases for combating environmental phosphate pollution and other diverse applications

Kumar

Chanderman

Makolomakwa

et al. 2015

Critical Reviews in Environmental Science and Technology

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Concerns of phosphorus pollution and its impact on environments have driven the biotechnological development of phytases. Phosphoric acid, inositol phosphate, or inositols are produced after hydrolysis of phosphate from phytate, initiated by phytase. Research over the last two decades on microbial phytases has deepened our understanding of their production, optimization, and characterization. Despite the wide availability of phytase producing microorganisms, only a few have been commercially exploited. The current high cost of phytases, inability to withstand high temperatures (>85 C), a limited pH range, and poor storage stability are a major bottleneck in the commercialization of phytases. The development of novel phytases with optimal properties for various applications is a major research challenge. In this paper, recent advances in microbial phytase production, application of tools to optimize higher enzyme production, and characterization of phytases along with potential biotechnological applications are reviewed. Additionally the development of phytase assay methods and functions of phytate and phytate degradation products are discussed.

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Thermostable alkaline phytase from Bacillus sp. MD2: Effect of divalent metals on activity and stability

Cited by 29 publications

References 29 publications

A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

A novel extracellular low‐temperature active phytase from Bacillus aryabhattai RS1 with potential application in plant growth

Degradation of Phytate Pentamagnesium Salt by Bacillus sp. T4 Phytase as a Potential Eco-friendly Feed Additive

Microbial production of phytases for combating environmental phosphate pollution and other diverse applications

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