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Thermostable Alkaline Phytase from Alcaligenes sp. in Improving Bioavailability of Phosphorus in Animal Feed: In Vitro Analysis.

Vijayaraghavan P, Primiya RR, Prakash Vincent SG - ISRN Biotechnol (2013)

Bottom Line: The optimum pH range and temperature for the activity of phytase were found to be 7.0-8.0 and 60°C, respectively.This enzyme was strongly inhibited by 0.005 M of Mn(2+), Mg(2+), and Zn(2+).In vitro studies revealed that the phytase from Alcaligenes sp. released inorganic phosphate from plant phytates.

View Article: PubMed Central - PubMed

Affiliation: Centre for Marine Science and Technology, Manonmaniam Sundaranar University, Rajakkamangalam, Kanyakumari, Tamil Nadu 629 502, India.

ABSTRACT
A bacterial isolate, Alcaligenes sp. secreting phytase (EC 3.1.3.8), was isolated and characterized. The optimum conditions for the production of phytase included a fermentation period of 96 h, pH 8.0, and the addition of 1% (w/v) maltose and 1% (w/v) beef extract to the culture medium. This enzyme was purified to homogeneity and had an apparent molecular mass of 41 kDa. The optimum pH range and temperature for the activity of phytase were found to be 7.0-8.0 and 60°C, respectively. This enzyme was strongly inhibited by 0.005 M of Mn(2+), Mg(2+), and Zn(2+). In vitro studies revealed that the phytase from Alcaligenes sp. released inorganic phosphate from plant phytates. Phytase released 1930 ± 28, 1740 ± 13, 1050 ± 31, 845 ± 7, 1935 ± 32, and 1655 ± 21 mg inorganic phosphate/kg plant phytates, namely, chick pea, corn, green pea, groundnut, pearl pea, and chick feed, respectively.

No MeSH data available.


Related in: MedlinePlus

Effect of pH on phytase activity and stability. The Alcaligenes sp. was inoculated in the minimal medium containing 1% (w/v) sodium phytate as the sole phosphorus source and incubated at 37°C for 144 h in an orbital shaker at 150 rpm. The result was the mean of three different repeats. Error bar standard deviation.
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fig2: Effect of pH on phytase activity and stability. The Alcaligenes sp. was inoculated in the minimal medium containing 1% (w/v) sodium phytate as the sole phosphorus source and incubated at 37°C for 144 h in an orbital shaker at 150 rpm. The result was the mean of three different repeats. Error bar standard deviation.

Mentions: In Alcaligenes sp. phytase activity was found to be high (100% activity) at pH 8.0. The relative enzyme activity was 0.9  ±  0.13%, 3.4  ±  0.18%, 44.5  ±  3.4, 98  ±  5.5%, and 40  ±  2.2% at pH 4.0, 5.0, 6.0, 7.0, and 9.0, respectively. This enzyme was also highly stable at pH 8.0 at which the relative enzyme activity was 100%. The relative enzyme activity was 0.4  ±  0.16, 40  ±  0.21, 47  ±  0.18, and 27  ±  0.24%, at pH 4.0, 5.0, 6.0, 7.0, and 9.0, respectively, (Figure 2). This property was in accordance with the previously reported results. Some bacterial phytases have broad pH optima but are shifted towards a more basic pH range [22, 23]. This enzyme was highly stable at pH 8.0 (100% relative activity).


Thermostable Alkaline Phytase from Alcaligenes sp. in Improving Bioavailability of Phosphorus in Animal Feed: In Vitro Analysis.

Vijayaraghavan P, Primiya RR, Prakash Vincent SG - ISRN Biotechnol (2013)

Effect of pH on phytase activity and stability. The Alcaligenes sp. was inoculated in the minimal medium containing 1% (w/v) sodium phytate as the sole phosphorus source and incubated at 37°C for 144 h in an orbital shaker at 150 rpm. The result was the mean of three different repeats. Error bar standard deviation.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4417553&req=5

fig2: Effect of pH on phytase activity and stability. The Alcaligenes sp. was inoculated in the minimal medium containing 1% (w/v) sodium phytate as the sole phosphorus source and incubated at 37°C for 144 h in an orbital shaker at 150 rpm. The result was the mean of three different repeats. Error bar standard deviation.
Mentions: In Alcaligenes sp. phytase activity was found to be high (100% activity) at pH 8.0. The relative enzyme activity was 0.9  ±  0.13%, 3.4  ±  0.18%, 44.5  ±  3.4, 98  ±  5.5%, and 40  ±  2.2% at pH 4.0, 5.0, 6.0, 7.0, and 9.0, respectively. This enzyme was also highly stable at pH 8.0 at which the relative enzyme activity was 100%. The relative enzyme activity was 0.4  ±  0.16, 40  ±  0.21, 47  ±  0.18, and 27  ±  0.24%, at pH 4.0, 5.0, 6.0, 7.0, and 9.0, respectively, (Figure 2). This property was in accordance with the previously reported results. Some bacterial phytases have broad pH optima but are shifted towards a more basic pH range [22, 23]. This enzyme was highly stable at pH 8.0 (100% relative activity).

Bottom Line: The optimum pH range and temperature for the activity of phytase were found to be 7.0-8.0 and 60°C, respectively.This enzyme was strongly inhibited by 0.005 M of Mn(2+), Mg(2+), and Zn(2+).In vitro studies revealed that the phytase from Alcaligenes sp. released inorganic phosphate from plant phytates.

View Article: PubMed Central - PubMed

Affiliation: Centre for Marine Science and Technology, Manonmaniam Sundaranar University, Rajakkamangalam, Kanyakumari, Tamil Nadu 629 502, India.

ABSTRACT
A bacterial isolate, Alcaligenes sp. secreting phytase (EC 3.1.3.8), was isolated and characterized. The optimum conditions for the production of phytase included a fermentation period of 96 h, pH 8.0, and the addition of 1% (w/v) maltose and 1% (w/v) beef extract to the culture medium. This enzyme was purified to homogeneity and had an apparent molecular mass of 41 kDa. The optimum pH range and temperature for the activity of phytase were found to be 7.0-8.0 and 60°C, respectively. This enzyme was strongly inhibited by 0.005 M of Mn(2+), Mg(2+), and Zn(2+). In vitro studies revealed that the phytase from Alcaligenes sp. released inorganic phosphate from plant phytates. Phytase released 1930 ± 28, 1740 ± 13, 1050 ± 31, 845 ± 7, 1935 ± 32, and 1655 ± 21 mg inorganic phosphate/kg plant phytates, namely, chick pea, corn, green pea, groundnut, pearl pea, and chick feed, respectively.

No MeSH data available.


Related in: MedlinePlus