Food Science and Biotechnology

  • 제16권4호
  • /
  • Pages.580-583
  • /
  • 2007
  • /
  • 1226-7708(pISSN)
  • /
  • 2092-6456(eISSN)
한국식품과학회 (Korean Society of Food Science and Technology)
권호 표지

Phytase Properties from Bifidobacterium animalis

  • Oh, Nam-Soon (Department of Food Science and Technology, Kongju National University) ;
  • Lee, Byong-Hoon (Department of Food Science and Agricultural Chemisty, McGill University)
  • 발행 : 2007.08.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

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.

키워드

참고문헌

  1. Konietzny U, Greiner R. Molecular and catalytic properties of phytate-degrading enzymes (phytase). Int. J. Food Sci. Tech. 37: 791-812 (2002) https://doi.org/10.1046/j.1365-2621.2002.00617.x
  2. Common FH. Biological availability of phosphorus for pigs. Nature 143: 370-380 (1989)
  3. Kerovuo J, Lauraeus M, Nurminen P, Kalkkinen N, Apajalahti J. Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis. Appl. Environ. Microb. 64: 2079-2085 (1998)
  4. Tye AJ, Siu FKY, Leung TYC, Lim BL. Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. lincheniformis. Appl. Microbiol. Biot. 59: 190-197 (2002) https://doi.org/10.1007/s00253-002-1033-5
  5. Gibson DM, Ullah AHJ. Purification and characterization of phytase from cotyledons of germinating soybean seeds. Arch. Biochem. Biophys. 260: 503-513 (1988) https://doi.org/10.1016/0003-9861(88)90475-4
  6. Greiner R. Purification and characterization of three phytases from germinated lupine seeds (Lupinus albus var. Amiga). J. Agr. Food Chem. 50: 6858-6864 (2002) https://doi.org/10.1021/jf025619u
  7. Mullaney EJ, Daly CB, Sethumadhavan K, Rodriquez E, Lei XG, Ullah AHJ. Phytase activity in Aspergillus fumigatus isolates. Biochem. Bioph. Res. Co. 275: 759-763 (2000) https://doi.org/10.1006/bbrc.2000.3234
  8. Ullah AHJ, Gibson DM. Extracellular phytase (E.C. 3.1.3.8) from Aspergillus ficuum NRRL 3135: Purification and characterization. Prep. Biochem. 17: 63-91 (1987) https://doi.org/10.1080/00327488708062477
  9. Choi YM, Noh DO, Cho SH, Lee HK, Suh SJ, Chung SH. Isolation of a phytase-producing Bacillus sp. KHU-10 and its phytase production. J. Microbiol. Biotechn. 9: 223-226 (1999)
  10. Greiner R, Konietzny U, Jany KD. Purification and characterization of two phytases from Escherichia coli. Arch. Biochem. Biophys. 303: 107-113 (1993) https://doi.org/10.1006/abbi.1993.1261
  11. In MJ, Jang ES, Kim YJ, Oh NS. Purification and properties of an extracellular acid phytase from Pseudomonas fragi Y9451. J. Microbiol. Biotechn. 14: 1004-1008 (2004)
  12. Kim YH, Gwon MN, Yang SY, Park TK, Kim CG, Kim CW, Song MD. Isolation of phytase-producing Pseudomonas sp. and optimization of its phytase production. J. Microbiol. Biotechn. 12: 279-285 (2002)
  13. Kim YJ, Jang ES, In MJ, Oh NS. Isolation of phytase producing Pseudomonas fragi and optimization of its phytase production. J. Korean Soc. Agric. Chem. Biotechnol. 46: 291-298 (2003)
  14. Zamudio M, Gonzalez A, Medina JA. Lactobacillus plantarum phytase is due to non-specific acid phosphatase. Lett. Appl. Microbiol. 32: 181-184 (2001) https://doi.org/10.1046/j.1472-765x.2001.00890.x
  15. Haros M, Bielecka M, Sanz Y. Phytase activity as a novel metabolic feature in Bifidobacterium. FEMS Microbiol. Lett. 247: 231-239 (2005) https://doi.org/10.1016/j.femsle.2005.05.008
  16. Holzapfel WH, Haberer P, Snel J, Schillinger U, Huis in't Veld JHJ. Overview of gut flora and probiotics. Int. J. Food Microbiol. 41: 85- 101 (1998) https://doi.org/10.1016/S0168-1605(98)00044-0
  17. Kim SJ. Potential probiotic properties of lactic acid bacteria isolated from kimchi. Food Sci. Biotechnol. 14: 547-550 (2005)
  18. Choi NY, Shin HS. Effect of oligosaccharides and inulin on the growth and viability of Bifidobacteria in skim milk. Food Sci. Biotechnol. 15: 543-548 (2006)
  19. Lim SI, Kim GB, Yi SH, Lee BH. Characteristics of a Bifidobacterium longum LL04 $\beta$-galactotosidase(recombinant) produced in Escherichia coli. Food Sci. Biotechnol. 15: 908-913 (2006)
  20. Shimizu M. Purification and characterization of phytase from Bacillus subtilis (natto) N-77. Biosci. Biotech. Bioch. 58: 1266- 1269 (1992)
  21. Heinonen JK, Lahti RJ. A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic phosphatase. Anal. Biochem. 113: 313-317 (1981) https://doi.org/10.1016/0003-2697(81)90082-8
  22. Ebune A, Asheh AS, Duvnjak Z. Effects of phosphate, surfactants and glucose on phytase production and hydrolysis of phytic acid in canola meal by Aspergillus ficum during solid state fermentation. Bioresource Technol. 54: 241-247 (1995) https://doi.org/10.1016/0960-8524(95)00133-6
  23. Seo SW, In MJ, Oh NS. Production and reaction properties of phytase by Saccharomyces cerevisiae CY strain. J. Korean Soc. Appl. Biol. Chem. 48: 228-232 (2005)