• Food Science and Biotechnology
• /
• v.16 no.4
• /
• pp.580-583
• /
• 2007

Phytase activity was examined with various bifidobacterial strains cultured statically in MRS broth at $37^{\circ}C$ for 48 hr. Seven Bifidobacterium species showed mostly an intracellular phytase activity, though their specific activities were very low. The highest specific activity was found in Bifidobacterium animalis B33 strain, among 7 bifidobacteria tested. The specific activity was highest during the exponential growth phase. Carbohydrates and the concentration of phosphorus sources had an effect on the phytase activity and bacterial growth. Glucose was the most favorable carbohydrate for the phytase activity. Phytate inhibited the cell growth, and phytase activity decreased with increase of phytate concentration. The phytase activity was even higher in the static microaerophilic growth than that in anaerobic state, despite the stimulated growth in anaerobic growth. The optimal pH ranges were comparatively broad, but the optimal temperatures were $50^{\circ}C$ for all tested strains. The phytase activity was most active at pH 6.5 and $50^{\circ}C$ for B. animalis B33 strain.

• Journal of Environmental Health Sciences
• /
• v.27 no.4
• /
• pp.1-8
• /
• 2001

From August 2000 to August 2001, 9 variables of physicochemical factors and phytase activity were investigated at 4 sites in the River Yungpyung and the influences of Physicochemical factors to Phytase activity were analyzed. Phytase activities of Site 1, Site 2, Site 3, and Site 4 varied between N.D ∼566 nmol/ ι /hr, N.D \" 434 nmol/ ι /hr, N.D ∼557 nmol/ ι /hr, and N.D ∼723 nmol/ ι /hr, respectively. The activities of summer season were higher than those of other season. But the activities were not detected on the winter season. The phytase activity and temperature showed high correlation. The correlation coefficients of Site 1, Site 2, Site 3, and Site 4 were 0.82(p<0.01).0.92(p<0.01),0.87(p<0.01), and 0.88(p<0.01), respectively. The phytase activity and NOI₃/sup -/ ion showed negative relation(r=-0.59, p<0.05) at Site 1. And the phytase activity had relation with Zn/sup 2+/at Site 2(r=().57, p<0.05) and Site 3(r=0.7E, p<7.07).

• Asian-Australasian Journal of Animal Sciences
• /
• v.15 no.7
• /
• pp.1036-1039
• /
• 2002

The effect of germination on phytase activity in wheat NEAU123, triticale5305 and rye2 was studied in the present study. Germination significantly increased phytase activity by 2.04 times for wheat NEAU123 (3 d), 1.82 times for triticale 5305 (1 d) and 2.45 times for rye2 (1 d), respectively. It was safe for phytase in fresh malts kilned for 2 h at $40^{\circ}C$. Phytase in cereal seeds had strong heat stability. There was no loss of phytase activity in cereal seeds heated at $70^{\circ}C$ for 1 h, a little loss (${\leq}$5.46%) at $80^{\circ}C$ or $90^{\circ}C$. Even heated at $100^{\circ}C$, the phytase activity in wheat NEAU123, triticale5305 and rye2 remained 89.47%, 86.44% and 104.64%, respectively.

• Mycobiology
• /
• v.33 no.4
• /
• pp.223-229
• /
• 2005

A novel fungal strain Aspergillus sp. L117 that produced acid-stable and thermostable phytase was isolated on basis of the clearing zone on PSM plate and the ability of Na-phytate hydrolysis. The phytase of isolate showed a 3-fold higher activity than that of A. ficuun NRRL3135. The Aspergillus sp. L117 produced maximal level of phytase at initial pH of 5.0 and $30^{\circ}C$. The optimal pH and temperature for phytase activity were 5.5 and $50^{\circ}C$, respectively. The phytase showed totally stable activity after 20 min of exposure between 30 and $90^{\circ}C$, and even at $100^{\circ}C$. The highest level of residual phytase activity was obtained at pH 5.5, and still retained the stability at the broadest pH ranges (2.0 to 7.0) of all the aforementioned phytases. Storage stability of phytase was preserved over 96% of initial activities for 60 days at 4, -20, and $-70^{\circ}C$ and to retain even 70% of the initial activity at room temperature.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.27 no.1
• /
• pp.38-45
• /
• 1998

To extract insoluble proteins and to improve funtional properties of abolished proteins, an phytase producing Aspergillus sp. SM-15 was isolated from soil. The enzyme was purified and its enzymological characteristics were investigated. Phytase production reached to maximum when the wheat bran medium containing 1% mannose, 1% yeast extract, 1% (NH4)2HPO4 and 0.2% calcium chloride was cultured for 4 days. Phytase was purified 17.1 fold and specific activity was 244.32unit/mg by a sequencial process of ammonium sulfate fraction, ion exchange chromatography and gel filtrations Pruified enzyme was confirmed as a single band by the polyacrylamide gel electro-phoresis. The molecular weight of phytase was estimated to be 46,000. The optimum pH and temperature for the phytase activity were 5.5 and 5$0^{\circ}C$. The enzyme is stable in pH 4.5~5.5, 6$0^{\circ}C$. The activity of purified enzyme was inhibited by Hg2+ whereas activited by Pb2+ and Fe2+. The activity of phytase was inhibited by the treatment with iodine. The result indicate the possible involvement of histidine at active site. Km and Vmax of the puridied phytase were 37.037mM/L and 159.87umol/min, respectively.

• Applied Biological Chemistry
• /
• v.48 no.3
• /
• pp.228-232
• /
• 2005

A yeast strain producing phytase, isolated from a mash of Korean traditional Yakju, was identified as a strain of Saccharomyces cerevisiae and designated as Saccharomyces cerevisiae CY strain. Phytase was produced by CY strain both intracellularly and extracellularly. Total phytase activity by the shaking culture was about two times higher than that of the static culture. The portion of extracellular phytase to total phytase activity ranged between 23 and 49 percent, depending on the glucose concentration in the culture medium. Phytase production was reached at approximately 1 U/ml as total phytase activity and the maximum intracellular phytase activity was 0.17-0.19 U/mg-DCW at late logarithmic growth phase. The optimum reaction pH and temperature of intracellular phytase were 3.5 and $40^{\circ}C$, respectively. Over 95% of the phytate was degraded by growing cells after 36 hours yeast cell culture and about 90% of total phytate was effectively degraded by suspending the whole cell with the biomass of 0.4 mg-DCW/ml-reaction solution after 12 hours degradation reaction.

• Journal of Animal Environmental Science
• /
• v.6 no.1
• /
• pp.45-52
• /
• 2000

The effect of earthworm on the recycling or control of organic P in environment has been investigated. The activity of phytase(myo-inositol hexaposphate phosphohydrolase, EC 3.1.3.8) produced by isolated microoganisms from vermicomposted cow manure was usually higher than that of phytase produced by isolated microorganisms from composted cow manure. However the activity of phytase excreted by seperated earthworm(Eisenia foetida) was not detected. The concentration of total P and available P was revealed 2.88%, 0.22% in composted cow manure and 1.70% 0.14% in vermicomposted cow manure.

• Journal of Life Science
• /
• v.7 no.2
• /
• pp.127-133
• /
• 1997

The phytase(myo-inositol hexkisphosphate phosphohydrolase ; EC 3.1.3.8) activity was observed only in the homogenate of intestinal mucosa, though the activity of alkaline phisphatase was measurable in various organs. In addition, no protein bands were detected in any other organs on immunoblotting using the anti-90kDa phytase antiserum. Thses results suggest that phytase is specifically present in small intestinal mucosa, and that hydrolysis of phytic acid(inositol-hexakisphosphate) can be allotted for a physiological role of the intestine-specific enzyme. The activities of phytase was increased during development of rat. The 70kDa phytase appeared just after birth, but the 90kDa phytase was not observed until adult period, suggesting that the 90kDa phytase was synthesized in response to weanling.

• Journal of Animal Science and Technology
• /
• v.61 no.2
• /
• pp.87-97
• /
• 2019

Phytate induced excessive mineral excretion through poultry litter leads to poor performance and environmental pollution. Exogenous microbial phytase supplementation to poultry diets reduce the environmental excretion of nutrient and improve bird's performance. However, excessive dietary sodium (Na) level may hinder the phytase-mediated phytate hydrolysis and negate the beneficial effects of phytase. Therefore, this experiment was conducted to investigate the effects of different concentration dietary Na on phytase activity and subsequent impact on broiler performance, bone mineralisation and nutrient utilisation. In this study, six experimental diets, consisting of three different levels of Na (1.5, 2.5, or 3.5 g/kg) and two levels of microbial phytase (0 or 500 U/kg) were formulated by using $3{\times}2$ factorial design. The six experimental diets were offered to 360 day-old Ross 306 male chicks for 35 days, where, each experimental diet consisted of 6 replicates groups with 10 birds. Along with growth performance, nutrient utilization, intestinal enzyme activity, dry matter (DM) content of litter and mineral status in bone were analysed. Dietary Na and phytase had no effect on bode weight gain and feed intake. Birds on the low Na diet showed higher (p < 0.05) feed conversion ratio (FCR) than the mid-Na diets. High dietary Na adversely affected (p < 0.001) excreta DM content. Phytase supplementation to the high-Na diet increased (p < 0.01) the litter ammonia content. High dietary Na with phytase supplementation improved ($Na{\times}phytase$, p < 0.05) the AME value and ileal digestibility of Ca and Mg. The total tract retention of Ca, P, and Mg was reduced with high Na diet, which was counteracted by phytase supplementation ($Na{\times}phytase$, p < 0.001). The diets containing mid-level of Na improved (p < 0.001) the function of Na-K-ATPase and Mg-ATPase in the jejunum. The overall results indicate that high dietary Na did not affect phytase activity but influenced the nutrient utilization of birds, which was not reflected in bird overall performance.

• Asian-Australasian Journal of Animal Sciences
• /
• v.13 no.7
• /
• pp.957-961
• /
• 2000

A series of experiments was conducted to evaluate phytin phosphohydrolysis actlVlty in the rumen and to isolate phytase positive rumen bacteria. Endogenous phytase activity of wheat bran was estimated and compared with that of bacterial phytin phosphohydrolysis. Substantial phytase activity was detected in wheat bran during in vitro rumen incubation. Bacterial phytase activity was suggested not to be high. Only two facultative anaerobes, Klebsiella sp. and Corynebacterium sp. were isolated as phytase producing organisms. These belonged to a minor microbial group in the rumen population. Protozoal fraction showed an initial velocity of phytin phosphohydrolysis 7 times higher than the bacterial fraction.