• Animal Bioscience
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• v.34 no.8
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• pp.1365-1374
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• 2021

Objective: This study was conducted to investigate the synergistic effect of exogenous multienzyme and phytase on growth performance, nutrients digestibility, blood metabolites, intestinal microflora, and morphology in broilers fed corn-wheat-soybean meal diets. Methods: A 2×2 factorial design was used in this study. Four dietary treatments consisted of i) basal diets (corn-wheat-soybean meal based diets without multi-enzyme and phytase), ii) basal diets with phytase (0.05%), iii) basal diets with exogenous multi-enzyme (0.05%), and iv) basal diets with exogenous multi-enzyme including phytase (0.05%). A total of 480 broiler chickens (Ross 308 - one day old) were weighed and allotted to thirty-two cages (15 birds per cage), and chicks were randomly allocated to four dietary treatments. Results: The body weight gain and feed conversion rate were improved by supplementation of exogenous multi-enzyme containing phytase during the finisher period (p<0.05). The birds fed diets with exogenous multi-enzyme containing phytase had a significantly greater digestibility of dry matter, gross energy, crude protein, calcium, and phosphorus compared with birds fed non-supplemented diets (p<0.05). The chickens fed diets with exogenous multi-enzyme containing phytase showed a higher concentration of Ca and P in the serum (p<0.05). The population of Lactobacillus spp., Escherichia coli, and Clostridium were not affected in the ileum and cecum of chickens fed enzyme-supplemented diets. The dietary supplemental exogenous multi-enzyme containing phytase showed a significant improvement in villus height, crypt depth, and villus height and crypt depth ratio, compared to basal diets or dietary supplemental phytase (p<0.05). Conclusion: The supplementation of the exogenous multi-enzyme containing phytase synergistically improved the growth performance, nutrients digestibility, and villus height of the small intestine of broiler chickens fed a corn-wheat-soybean meal based diets.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.1
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• pp.57-63
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• 2000

To extract insoluble proteins from abolished soybean meal, the meal was treatesd with phytase and protease produced by Aspergillus sp. SM-15 and Aspergillus sp. MS-18. The extraction of insoluble soybean protein was increased at alkaline range more than pH 5 in case of phytase, pH 7 to 11 in case of protease and pH 5 to 12 in case of the mixed enzyme of phytase and protease. The optimum extraction temperature of insoluble protein was 5$0^{\circ}C$ for phytase and the mixed enzyme of phytase and protease, and 6$0^{\circ}C$ for protease. The optimum treatment time for extraction of protein was 9 hrs for phytase, 11 hrs for protease and the mixed enzyme of phytase and protease and optimum unit of enzyme for extraction of protein was 600 unit, 40 unit and 900 unit＋60 unit in case of phytase, protease, phytase and protease, respectively. The treatment of mixed enzyme showed higher extracton rate of protein than single enzyme treatment. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of soybean meal protein by the treatment of the enzymes increased at all pH range. Further more oil absorption as well as water absorption capacities by the treatment of the enzymes were also increased. The functional properteis of the soybean meal protein treated by the mixed enzyme were higher than those of soybean meal protein treated by the single enzyme.

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

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.4
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• pp.523-532
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• 2004

An experiment was conducted to investigate the effect of microbial phytase ($Natuphos^{R}$) supplementation in combination with enzyme complex (composed of enzymes targeted to SBM dietary components such as $\alpha$-galactosides and galactomannans; $Endo-Power^{R}$) to diet with low nutrient levels on growth performance and ileal nutrient digestibility of weaned pigs. A total of 210 crossbred weaned pigs (Landrace$\times$Yorkshire$\times$Duroc), 6.68$\pm$0.98 kg of initial body weight, were randomly allotted to five dietary treatments, based on weight and age, according to a randomized complete block design. There were three pens per treatment and 14 pigs per pen. The dietary treatments were 1) CON (Control diet with no phytase and enzyme complex (EC)), 2) LP+EC 100 (Control diet with 0.15% unit lower available phosphorus (aP) level+0.1% phytase (500 FTU/kg diet) and 0.1% enzyme complex), 3) LP+EC 80 (Control diet with 0.15% unit lower aP level+0.08% phytase (400 FTU/kg diet) and 0.08% enzyme complex, 4) LPEA+EC 100 (Control diet with 0.15% unit lower aP and 3% lower ME and amino acid levels (lysine, methionine, threonine and typtophan)+0.1% phytase (500 FTU/kg diet) and 0.1% enzyme complex), 5) LPEA+EC 80 (Control diet with 0.15% unit lower aP and 3% lower ME and amino acid levels+0.08% phytase (400 FTU/ kg diet) and 0.08% enzyme complex). For the determination of ileal nutrients digestibility, a total of 15 T-cannulated pigs (initial body weight; 7.52$\pm$1.24 kg; 3 replicates per treatment) were used in the present study. Piglets were weighted and allotted into same dietary treatments as one in growth trial and phase I experimental diets were provided for ileal digestibility study. There was no significant difference (p>0.05) in average daily gain (ADG) and average daily feed intake (ADFI) among dietary treatments during the whole experimental period (0 to 5 weeks). However, piglets in LP+EC 100 group had a significantly higher gain/feed ratio (G:F) than piglets had in control (p<0.05). Crude protein, energy and phosphorus digestibilities were significantly improved when both of phytase and enzyme complex were supplemented at the revel of 0.1%, respectively to diets with low nutrient level (aP or (and) ME and amino acids) (p<0.05). Piglets in LP+EC 100 and LPEA+EC 100 groups showed significantly higher phosphorus content (%) in bone than that of piglets in control group (p<0.05). Supplementation of both of phytase and enzyme complex at 0.1%, respectively, to diet with low nutrient levels (aP or (and) ME and amino acids) significantly improved total ileal essential amino acid and nonessential amino acid digestibilities compared to control group (p<0.05). In conclusion, the results from the present study suggest that the simultaneous inclusion of phytase and enzyme complex to diets at recommended level is advantageous with respect to improving growth performance and nutrient digestibility of weaned pigs and may contribute to increased economic return when added to corn-soy based weaned pig diets.

• Asian-Australasian Journal of Animal Sciences
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• v.18 no.10
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• pp.1457-1463
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• 2005

In this research, the possibilities of using canola meal (CM) in place of soybean meal (SBM), and also the effects of multi-enzyme and phytase supplementation on the performance of quails were investigated. For this purpose, soybean meal (44% CP), canola meal (37% CP), phytase (produced from Peniophora luci) and multi-enzyme ($\beta$-glucanases, pectinases, cellulases and hemicellulases) were used. CM was used supplying 0, 25 and 50% of CP from SBM and each of the phytase and multi-enzyme blends were added to the each level. This study was conducted with 675 day old quails (Coturnix coturnix Japonica) in 9 groups with 3 replicates including 25 birds (mixed sex) per replicate. Nine isocalaric and isonitrogenous diets were prepared. The effects of enzymes and CM levels were studied with a 3${\times}$3${\times}$3 factorial arrangement for three CM levels (0, 25 and 50%), three treatments (without enzyme, phytase enzyme and multi-enzyme) and three replicates. While the 25% CM level did not affect the liveweight gain 50% CM level decreased the liveweight gain (p<0.05). Multi-enzyme addition to the 50% CM group increased the liveweight gain compared to the other groups (p<0.05). CM levels and enzyme supplementation had no effect on feed consumption, feed conversion ratio, dressing percentage, viability, tibia ash content, Ca and P contents of tibia ash, viscera weight, gizzard weight and length of growth period. While heart weight and liver weight were not affected by CM levels, but they were affected by enzyme supplementation. CM levels and enzyme supplementation did not affect final liveweight, feed consumption, feed conversion ratio, egg yield, egg weight, shell weight and shell index during laying period. The increase in the CM level lightened the colour of the yolk (p<0.05).

• Food Science and Biotechnology
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• v.18 no.3
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• pp.655-660
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• 2009

Biotechnological phytase preparations are commercially available and are currently used in animal feeding. However, thermostability constraints, low yields, and the high cost of the enzyme have limited its use. This study represents a new perspective for the food enzyme market. The research screened thermostable yeast strains for their ability to produce phytase. The screening was carried out with a gradual increase in temperature ($30-48^{\circ}C$). Sixteen strains (1 strain identified as Saccharomyces cerevisiae) maintained the ability to produce phytase at $48^{\circ}C$ and their phytase activity was confirmed using 2 phytase assay methodologies. The yeast strains tested in this study seem to be potential efficient producers of phytase, indicating a possible new source of thermostable phytase of commercial interest, particularly that from S. cerevisiae.

• Journal of Life Science
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• v.7 no.2
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• pp.127-133
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• 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 Life Science
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• v.7 no.2
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• pp.119-126
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• 1997

Phytase(myo-inositol hexkisphosphate phosphohydrolase ; EC 3.1.3.8) was purified from the mucoas of rat intestinal. The molecular weight of enzyme was determined to be 160kDa by sephacryl S-200 gel filtration. Analysis of the purified enzyme o SDS-polyacrylamide gel electrophoresis(SDS-PAGE) showen that it was composed of two different subunits and the molecular weight of its subunit was found to be 70kDa and 90kDa respectively, indicating that this enzyme is hetrodimer. The enzyme activities were activated in the presence of $ MgCl_{2}$, but inhibited by $ZnCl_{2}$, $MnCl_{2}$, and EDTA. The substrates tested, phytase showed the highest affinity for the enzyme at the physiological ph. The Km value for phytic acid(inositol-hexakisphosphate)was 0.31 mM at pH 7.4. rat intestinal mucosa phytase seems to play an important in the metabolism of inositol.

• Journal of Microbiology and Biotechnology
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• v.15 no.4
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• pp.745-748
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• 2005

A phytase from Aeromonas sp. LIK 1-5 was partially purified by ammonium sulfate precipitation and DEAE-Sephacel column chromatography. Its molecular weight was 44 kDa according to SDS-PAGE gel. Enzyme activity was optimal at pH 7 and at $50^{\circ}C$. The purified enzyme was strongly inhibited by 2 mM EDTA, $Zn^{2+},\;Co^{2+},\;or\;Mn^{2+}$, and activated by 2 mM $Ca^{2+}$. The K_m value for sodium phytate was 0.23 mM, and the enzyme was resistant to trypsin. The N-terminal amino acid sequence of the phytase was similar to that of other known alkaline phytases. The phytase was specific for ATP and sodium phytate, which is different from other known alkaline phytases. Based on the substrate specificity, the phytase may therefore be a novel alkaline phytase.

• Microbiology and Biotechnology Letters
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• v.34 no.1
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• pp.28-34
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• 2006

A native extracellular acid phosphatase, phytase (EC 3.1.3.8), from Bacillus coagulans IDCC 1201 (commercially known as Lactobacillus sporogenes) used as probiotics, was characterized. Though some strains of B. coagulans have been evaluated with regard to several health-promoting effects, it has not been reported to produce phytase. Partially purified phytase front the strain IDCC 1201 had a pH optimum of 4.0 and a temperature optimum of $50^{\circ}C$, respectively. The requirement for divalent cations was studied and cobalt ion remarkably increased the enzyme activity. The removal of metal ions from the enzyme by EDTA decreased activity below 50%. The enzyme activity depleted restored when the assay was performed in the presence of $Co^{2+}$. Also, $Co^{2+}$ is the most active stimulator and has unique activation effect at high temperature. The phytase was specific for sodium phytate and p-nitrophenylphosphate, which is different from other known Bacilli phytases. The putative amino acid sequences of the phytase from B. coagulans IDCC 1201 were very similar to that of the phytase from B. subtilis strain 168. Based on these data, we concluded that the phytase from B. coagulans IDCC 1201 is a $Co^{2+}$-dependent acid phosphatase. Therefore, the strain B. coagulans IDCC 1201 is thought to be a valuable addititive for livestocks as well as a beneficial probiotics for human.