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Purification and Properties of Extracellular Phytase from Bacillus sp. KHU-10

Purification and Properties of Extracellular Phytase from Bacillus sp. KHU-10,10.1023/A:1010945416862,Journal of Protein Chemistry,Yang Mun Choi,Hyung

Purification and Properties of Extracellular Phytase from Bacillus sp. KHU-10   (Citations: 18)
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Bacillus species producing a thermostable phytase was isolated from soil, boiled rice, and mezu (Korean traditinal koji). The activity of phytase increased markedly at the late stationary phase. An extracellular phytase from Bacillus sp. KHU-10 was purified to homogeneity by acetone precipitation and DEAE-Sepharose and phenyl-Sepharose column chromatographies. Its molecular weight was estimated to be 46 kDa on gel filtration and 44 kDa on SDS-polyacrylamide gel elctrophoresis. Its optimum pH and temperature for phytase activity were pH 6.5-8.5 and 40°C without 10 mM CaCl2 and pH 6.0-9.5 and 60°C with 10 mM CaCl2. About 50% of its original activity remained after incubation at 80°C or 10 min in the presence of 10 mM CaCl2. The enzyme activity was fairly stable from pH 6.5 to 10.0. The enzyme had an isoelectric point of 6.8. As for substrate specificity, it was very specific for sodium phytate and showed no activity on other phosphate esters. The Km value for sodium phytate was 50 µM. Its activity was inhibited by EDTA and metal ions such as Ba2+, Cd2+, Co2+, Cr3+, Cu2+, Hg2+, and Mn2+ ions.
Journal: Journal of Protein Chemistry - J PROTEIN CHEM , vol. 20, no. 4, pp. 287-292, 2001
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    • ...A large number of fungal and bacterial phytases have been isolated, cloned and expressed in different hosts, and their properties have also been investigated (Ha et al. 2000; Choi et al. 2001; Tye et al. 2002; Mukesh et al. 2004; Cao et al. 2007; Lee et al. 2007; Soni and Khire 2007; Fu et al. 2008a, b, c; Guo et al. 2008; Hang et al. 2009; Mullaney et al. 2010; Tian et al. 2010)...
    • ...Recent research found that BPPs, which were first identified in the Bacillus species, having neutral to alkaline pH optimum (Choi et al. 2001; Tye et al. 2002; Oh et al. 2004; Gulati et al. 2007; Fu et al. 2008b), were potential candidates for hydrolysis of phytate in fish additive...

    Qian Wanget al. Characterization of a thermostable alkaline phytase from Bacillus lich...

    • ...This eliminates the need for external addition of phosphorous to the feed, which incurs costs and also contributes to environmental pollution [3, 23, 43]...
    • ...Removal of phytate from the feed also has other advantages in terms of overcoming its negative nutritional eVects such as decrease in the bioavailability of vital minerals [20, 21, 27, 30], impairing the function of digestive enzymes or decrease in the digestibility of feed protein [2, 3, 17]...

    Thi Thuy Tranet al. A thermostable phytase from Bacillus sp. MD2: cloning, expression and ...

    • ...Phytate-degrading enzymes have been detected in various bacteria, such as Bacillus sp. (Powar and Jagannatahan, 1982 and Shimizu, 1992; Keruvuo et al., 1998; Kim et al., 1998; Choi et al., 2001; Anis Shobirin, 2008), Citrobacter braakii (Kim et al., 2003), Enterobacter sp. (Yoon et al., 1996; Anis Shobirin, 2008) Escherichia coli (Greiner et al., 1993), Pseudomonas sp. (Irving and Cosgrove, 1971; Richardson and Hadobas, 1997), Raoultella ...

    Anis Shobirinet al. PHYTATE-DEGRADING ENZYME AND ITS POTENTIAL BIOTECHNOLOGICAL APPLICATIO...

    • ...This enzyme has no activity on the other compounds tested (Table 2). It should be noticed that phytases, from B. amyloliquefaciens DS11, B. subtilis 2712, and B. Sp. KHU-10, have been reported to be active exclusively on sodium phytate [17, 22, 25]...

    Ameny Farhatet al. Gene Cloning and Characterization of a Thermostable Phytase from Bacil...

    • ...The observed production pattern was ascribed to either a nutrient or energy limitation known to occur in the stationary phase as trigger for phytase production [9]...
    • ...The enzyme exhibited a speciWc activity of 12.69 U/mg proteins (Table 2). The partially puriWed preparation on SDS-PAGE showed two bands corresponding to 41 and 46 kDa (Fig. 6). Earlier reports on the puriWed phytase from Bacillus sp. KHU-10, B. subtilis (natto) N-77, B. subtilis, B. amyloliquefaciens had estimated the molecular weight (Mr) of 44, 33.8, 36, and 44 kDa [9, 22, 28, 32], respectively...
    • ...Pneumoniae XY-5, and E. coli exhibited strict substrate speciWcity for phytate esters [9, 13, 18, 22, 28, 36].The phytase from B. laevolacticus, however, showed relaxed substrate speciWcity and registered activities between (5.08–40%) against p-nitro-phenyl-phosphate, AMP, ATP, phenyl phosphate, and NaDPH2.Na4 (Table 3). The apparent K m and V max for the hydrolysis of partially puriWed phytase against sodium phytate was determined to be ...
    • ...The Km values of other phytases for sodium phytate from B. subtilis (natto) [32], Bacillus sp. DSII [22], and Bacillus KHU-10 [9] has also been reported in the same range...
    • ...Bacillus sp. KHU-10 0.160 Choi et al. [9] Bacillus amyloliquefaciens...

    H. K. Gulatiet al. Production and characterization of thermostable alkaline phytase from ...

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