메뉴 건너뛰기




Volumn 100, Issue 5, 2016, Pages 2225-2241

Identification and characterization of a mesophilic phytase highly resilient to high-temperatures from a fungus-garden associated metagenome

Author keywords

Heat resilient; Mesophilic; Metagenomic; Overexpression; Phytase

Indexed keywords

AMINO ACIDS; BIOINFORMATICS; CULTIVATION; ESCHERICHIA COLI; PHOSPHATASES;

EID: 84958939538     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-7097-9     Document Type: Article
Times cited : (33)

References (98)
  • 1
    • 84920901773 scopus 로고    scopus 로고
    • The efficacy of a new 6-phytase obtained from Buttiauxella spp. expressed in Trichoderma reesei on digestibility of amino acids, energy, and nutrients in pigs fed a diet based on corn, soybean meal, wheat middlings, and corn distillers’ dried grains with solubles
    • PID: 25568365
    • Adedokun SA, Owusu-Asiedu A, Ragland D, Plumstead P, Adeola O (2015) The efficacy of a new 6-phytase obtained from Buttiauxella spp. expressed in Trichoderma reesei on digestibility of amino acids, energy, and nutrients in pigs fed a diet based on corn, soybean meal, wheat middlings, and corn distillers’ dried grains with solubles. J Anim Sci 93:168–175. doi:10.2527/jas.2014-7912
    • (2015) J Anim Sci , vol.93 , pp. 168-175
    • Adedokun, S.A.1    Owusu-Asiedu, A.2    Ragland, D.3    Plumstead, P.4    Adeola, O.5
  • 3
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling
    • PID: 16301204
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:195–201. doi:10.1093/bioinformatics/bti770
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 5
    • 76349089524 scopus 로고    scopus 로고
    • Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme
    • PID: 20392204
    • Böhm K, Herter T, Müller JJ, Borriss R, Heinemann U (2010) Crystal structure of Klebsiella sp. ASR1 phytase suggests substrate binding to a preformed active site that meets the requirements of a plant rhizosphere enzyme. FEBS J 277:1284–1296. doi:10.1111/j.1742-4658.2010.07559.x
    • (2010) FEBS J , vol.277 , pp. 1284-1296
    • Böhm, K.1    Herter, T.2    Müller, J.J.3    Borriss, R.4    Heinemann, U.5
  • 6
    • 84922515281 scopus 로고    scopus 로고
    • Extraction of extracellular lipids from chemoautotrophic bacteria Serratia sp. ISTD04 for production of biodiesel
    • PID: 24650615
    • Bharti RK, Srivastava S, Thakur IS (2014) Extraction of extracellular lipids from chemoautotrophic bacteria Serratia sp. ISTD04 for production of biodiesel. Bioresour Technol 165:201–204. doi:10.1016/j.biortech.2014.02.075
    • (2014) Bioresour Technol , vol.165 , pp. 201-204
    • Bharti, R.K.1    Srivastava, S.2    Thakur, I.S.3
  • 8
    • 84903600211 scopus 로고    scopus 로고
    • The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization
    • PID: 24337251
    • Borgi M, Boudebbouze S, Aghajari N, Szukala F, Pons N, Maguin E, Rhimi M (2014) The attractive recombinant phytase from Bacillus licheniformis: biochemical and molecular characterization. Appl Microbiol Biotechnol 98:5937–5947. doi:10.1007/s00253-013-5421-9
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 5937-5947
    • Borgi, M.1    Boudebbouze, S.2    Aghajari, N.3    Szukala, F.4    Pons, N.5    Maguin, E.6    Rhimi, M.7
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding
    • PID: 942051
    • Bradford MM (1976) A rapid and sensitive method for the quantization of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. doi:10.1016/0003-2697(76)90527-3
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 84899623393 scopus 로고    scopus 로고
    • Increased understanding of the cereal phytase complement for better mineral bio-availability and resource management
    • Brinch-Pedersen H, Madsen CK, Holme IB, Dionisio G (2014) Increased understanding of the cereal phytase complement for better mineral bio-availability and resource management. J Cereal Sci 59:373–381. doi:10.1016/j.jcs.2013.10.003
    • (2014) J Cereal Sci , vol.59 , pp. 373-381
    • Brinch-Pedersen, H.1    Madsen, C.K.2    Holme, I.B.3    Dionisio, G.4
  • 11
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • PID: 14966662
    • Choi JH, Lee SY (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64:625–635. doi:10.1007/s00253-004-1559-9
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 13
    • 84899459039 scopus 로고    scopus 로고
    • Association between digesta pH, body weight, and nutrient utilization in chickens of different body weights and at different ages
    • Dono ND, Sparks NH, Olukosi OA (2014) Association between digesta pH, body weight, and nutrient utilization in chickens of different body weights and at different ages. J Poultry Sci 51:180–184. doi:10.2141/jpsa.0120151
    • (2014) J Poultry Sci , vol.51 , pp. 180-184
    • Dono, N.D.1    Sparks, N.H.2    Olukosi, O.A.3
  • 14
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • PID: 17446895
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H (2007) Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2:953–971. doi:10.1038/nprot.2007.131
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 15
    • 41149142244 scopus 로고    scopus 로고
    • A highly pH-stable phytase from Yersinia kristeensenii: cloning, expression, and characterization
    • Fu D, Huang H, Luo H, Wang Y, Yang P, Meng K, Bai Y, Wu N, Yao B (2008) A highly pH-stable phytase from Yersinia kristeensenii: cloning, expression, and characterization. Enzyme Microb Technol 42:499–505. doi:10.1016/j.enzmictec.2008.01.014
    • (2008) Enzyme Microb Technol , vol.42 , pp. 499-505
    • Fu, D.1    Huang, H.2    Luo, H.3    Wang, Y.4    Yang, P.5    Meng, K.6    Bai, Y.7    Wu, N.8    Yao, B.9
  • 17
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: status report and future prospects
    • PID: 16095898
    • Georgiou G, Segatori L (2005) Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr Opin Biotechnol 16:538–545. doi:10.1016/j.copbio.2005.07.008
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 18
    • 84964285927 scopus 로고    scopus 로고
    • Purification, biochemical characterization, and genetic cloning of the phytase produced by Burkholderia sp. strain a13
    • PID: 25833676
    • Graminho ER, Takaya N, Nakamura A, Hoshino T (2015) Purification, biochemical characterization, and genetic cloning of the phytase produced by Burkholderia sp. strain a13. J Gen Appl Microbiol 61:15–23. doi:10.2323/jgam.61.15
    • (2015) J Gen Appl Microbiol , vol.61 , pp. 15-23
    • Graminho, E.R.1    Takaya, N.2    Nakamura, A.3    Hoshino, T.4
  • 19
    • 70350142630 scopus 로고    scopus 로고
    • Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9
    • PID: 24031427
    • Greiner R, da Silva LG, Couri S (2009) Purification and characterisation of an extracellular phytase from Aspergillus niger 11T53A9. Braz J Microbiol 40:795–807. doi:10.1590/S1517-83822009000400010
    • (2009) Braz J Microbiol , vol.40 , pp. 795-807
    • Greiner, R.1    da Silva, L.G.2    Couri, S.3
  • 21
    • 67649890960 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of a novel phytase from Dickeya paradisiaca
    • PID: 18679591
    • Gu W, Huang H, Meng K, Yang P, Fu D, Luo H, Wang Y, Yao B, Zhan Z (2009) Gene cloning, expression, and characterization of a novel phytase from Dickeya paradisiaca. Appl Biochem Biotechnol 157:113–123. doi:10.1007/s12010-008-8329-6
    • (2009) Appl Biochem Biotechnol , vol.157 , pp. 113-123
    • Gu, W.1    Huang, H.2    Meng, K.3    Yang, P.4    Fu, D.5    Luo, H.6    Wang, Y.7    Yao, B.8    Zhan, Z.9
  • 22
    • 33845602128 scopus 로고    scopus 로고
    • Production and characterization of thermostable alkaline phytase from Bacillus laevolacticus isolated from rhizosphere soil
    • PID: 16967265
    • Gulati HK, Chadha BS, Saini HS (2007a) Production and characterization of thermostable alkaline phytase from Bacillus laevolacticus isolated from rhizosphere soil. J Ind Microbiol Biotechnol 34:91–98. doi:10.1007/s10295-006-0171-7
    • (2007) J Ind Microbiol Biotechnol , vol.34 , pp. 91-98
    • Gulati, H.K.1    Chadha, B.S.2    Saini, H.S.3
  • 23
    • 34447547676 scopus 로고    scopus 로고
    • Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7
    • PID: 17899792
    • Gulati HK, Chadha BS, Saini HS (2007b) Production, purification and characterization of thermostable phytase from thermophilic fungus Thermomyces lanuginosus TL-7. Acta Microbiol Immunol Hung 54:121–138. doi:10.1556/AMicr.54.2007.2.3
    • (2007) Acta Microbiol Immunol Hung , vol.54 , pp. 121-138
    • Gulati, H.K.1    Chadha, B.S.2    Saini, H.S.3
  • 24
    • 70349685126 scopus 로고    scopus 로고
    • Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241
    • PID: 19506861
    • Guo B, Chen X-L, Sun C-Y, Zhou B-C, Zhang Y-Z (2009) Gene cloning, expression and characterization of a new cold-active and salt-tolerant endo-β-1,4-xylanase from marine Glaciecola mesophila KMM 241. Appl Microbiol Biotechnol 84:1107–1115. doi:10.1007/s00253-009-2056-y
    • (2009) Appl Microbiol Biotechnol , vol.84 , pp. 1107-1115
    • Guo, B.1    Chen, X.-L.2    Sun, C.-Y.3    Zhou, B.-C.4    Zhang, Y.-Z.5
  • 25
    • 0019830545 scopus 로고
    • A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • PID: 6116463
    • Heinonen JK, Lahti RJ (1981) A new and convenient colorimetric determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal Biochem 113:313–317. doi:10.1016/0003-2697(81)90082-8
    • (1981) Anal Biochem , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahti, R.J.2
  • 26
    • 84924040634 scopus 로고    scopus 로고
    • Enhancement of thermostability and kinetic efficiency of Aspergillus niger PhyA phytase by site-directed mutagenesis
    • PID: 25527139
    • Hesampour A, Siadat SER, Malboobi MA, Mohandesi N, Arab SS, Ghahremanpour MM (2015) Enhancement of thermostability and kinetic efficiency of Aspergillus niger PhyA phytase by site-directed mutagenesis. Appl Biochem Biotechnol 175:2528–2541. doi:10.1007/s12010-014-1440-y
    • (2015) Appl Biochem Biotechnol , vol.175 , pp. 2528-2541
    • Hesampour, A.1    Siadat, S.E.R.2    Malboobi, M.A.3    Mohandesi, N.4    Arab, S.S.5    Ghahremanpour, M.M.6
  • 27
    • 84905974091 scopus 로고    scopus 로고
    • Overexpression and biochemical characterization of a thermostable phytase from Bacillus subtilis US417 in Pichia pastoris
    • PID: 24859267
    • Hmida-Sayari A, Elgharbi F, Farhat A, Rekik H, Blondeau K, Bejar S (2014) Overexpression and biochemical characterization of a thermostable phytase from Bacillus subtilis US417 in Pichia pastoris. Mol Biotechnol 56:839–848. doi:10.1007/s12033-014-9764-y
    • (2014) Mol Biotechnol , vol.56 , pp. 839-848
    • Hmida-Sayari, A.1    Elgharbi, F.2    Farhat, A.3    Rekik, H.4    Blondeau, K.5    Bejar, S.6
  • 28
    • 33750048736 scopus 로고    scopus 로고
    • A novel phytase with preferable characteristics from Yersinia intermedia
    • PID: 17034758
    • Huang H, Luo H, Yang P, Meng K, Wang Y, Yuan T, Bai Y, Yao B (2006) A novel phytase with preferable characteristics from Yersinia intermedia. Biochem Biophys Res Commun 350:884–889. doi:10.1016/j.bbrc.2006.09.118
    • (2006) Biochem Biophys Res Commun , vol.350 , pp. 884-889
    • Huang, H.1    Luo, H.2    Yang, P.3    Meng, K.4    Wang, Y.5    Yuan, T.6    Bai, Y.7    Yao, B.8
  • 29
    • 67349257141 scopus 로고    scopus 로고
    • A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive
    • PID: 19139877
    • Huang H, Shao N, Wang Y, Luo H, Yang P, Zhou Z, Zhan Z, Yao B (2009a) A novel beta-propeller phytase from Pedobacter nyackensis MJ11 CGMCC 2503 with potential as an aquatic feed additive. Appl Microbiol Biotechnol 83:249–259. doi:10.1007/s00253-008-1835-1
    • (2009) Appl Microbiol Biotechnol , vol.83 , pp. 249-259
    • Huang, H.1    Shao, N.2    Wang, Y.3    Luo, H.4    Yang, P.5    Zhou, Z.6    Zhan, Z.7    Yao, B.8
  • 30
    • 62149115657 scopus 로고    scopus 로고
    • Diversity of beta-propeller phytase genes in the intestinal contents of grass carp provides insight into the release of major phosphorus from phytate in nature
    • PID: 19151187
    • Huang H, Shi P, Wang Y, Luo H, Shao N, Wang G, Yang P, Yao B (2009b) Diversity of beta-propeller phytase genes in the intestinal contents of grass carp provides insight into the release of major phosphorus from phytate in nature. Appl Environ Microbiol 75:1508–1516. doi:10.1128/AEM.02188-08
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1508-1516
    • Huang, H.1    Shi, P.2    Wang, Y.3    Luo, H.4    Shao, N.5    Wang, G.6    Yang, P.7    Yao, B.8
  • 31
    • 79952092709 scopus 로고    scopus 로고
    • Diversity, abundance and characterization of ruminal cysteine phytases suggest their important role in phytate degradation
    • PID: 21105982
    • Huang H, Zhang R, Fu D, Luo J, Li Z, Luo H, Shi P, Yang P, Diao Q, Yao B (2011) Diversity, abundance and characterization of ruminal cysteine phytases suggest their important role in phytate degradation. Environ Microbiol 13:747–757. doi:10.1111/j.1462-2920.2010.02379.x
    • (2011) Environ Microbiol , vol.13 , pp. 747-757
    • Huang, H.1    Zhang, R.2    Fu, D.3    Luo, J.4    Li, Z.5    Luo, H.6    Shi, P.7    Yang, P.8    Diao, Q.9    Yao, B.10
  • 32
    • 77955474497 scopus 로고    scopus 로고
    • A quick guide to large-scale genomic data mining
    • Huttenhower C, Hofmann O (2010) A quick guide to large-scale genomic data mining. PLoS Comp Biol 6:e1000779. doi:10.1371/journal.pcbi.1000779
    • (2010) PLoS Comp Biol , vol.6 , pp. e1000779
    • Huttenhower, C.1    Hofmann, O.2
  • 33
    • 84880773351 scopus 로고    scopus 로고
    • Construction of a starch-inducible homologous expression system to produce cellulolytic enzymes from Acremonium cellulolyticus
    • PID: 23700177
    • Inoue H, Fujii T, Yoshimi M, Taylor LE II, Decker SR, Kishishita S, Nakabayashi M, Ishikawa K (2013) Construction of a starch-inducible homologous expression system to produce cellulolytic enzymes from Acremonium cellulolyticus. J Ind Microbiol Biotechnol 40:823–830. doi:10.1007/s10295-013-1286-2
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 823-830
    • Inoue, H.1    Fujii, T.2    Yoshimi, M.3    Taylor, L.E.4    Decker, S.R.5    Kishishita, S.6    Nakabayashi, M.7    Ishikawa, K.8
  • 34
    • 0015417183 scopus 로고
    • Inositol phosphate phosphatases of microbiological origin: the inositol pentaphosphate products of Aspergillus ficuum phytases
    • PID: 4342816
    • Irving GCJ, Cosgrove DJ (1972) Inositol phosphate phosphatases of microbiological origin: the inositol pentaphosphate products of Aspergillus ficuum phytases. J Bacteriol 112:434–438
    • (1972) J Bacteriol , vol.112 , pp. 434-438
    • Irving, G.C.J.1    Cosgrove, D.J.2
  • 35
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • PID: 9914256
    • Jaenicke R, Bohm G (1998) The stability of proteins in extreme environments. Curr Opin Struct Biol 8:738–748. doi:10.1016/s0959-440x(98)80094-8
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 36
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • PID: 8791626
    • Jaenicke R, Schurig H, Beaucamp N, Ostendorp R (1996) Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv Protein Chem 48:181–269. doi:10.1016/S0065-3233(08)60363-0
    • (1996) Adv Protein Chem , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 37
    • 0035936616 scopus 로고    scopus 로고
    • Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case
    • PID: 11164958
    • Jermutus L, Tessier M, Pasamontes L, van Loon A, Lehmann M (2001) Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case. J Biotechnol 85:15–24. doi:10.1016/s0168-1656(00)00373-4
    • (2001) J Biotechnol , vol.85 , pp. 15-24
    • Jermutus, L.1    Tessier, M.2    Pasamontes, L.3    van Loon, A.4    Lehmann, M.5
  • 38
    • 84894038809 scopus 로고    scopus 로고
    • Use of quantitative real-time PCR for direct detection of Serratia marcescens in marine and other aquatic environments
    • PID: 24375136
    • Joyner J, Wanless D, Sinigalliano CD, Lipp EK (2014) Use of quantitative real-time PCR for direct detection of Serratia marcescens in marine and other aquatic environments. Appl Environ Microbiol 80:1679–1683. doi:10.1128/aem.02755-13
    • (2014) Appl Environ Microbiol , vol.80 , pp. 1679-1683
    • Joyner, J.1    Wanless, D.2    Sinigalliano, C.D.3    Lipp, E.K.4
  • 39
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • PID: 18372315
    • Katoh K, Toh H (2008) Recent developments in the MAFFT multiple sequence alignment program. Brief Bioinform 9:286–298. doi:10.1093/bib/bbn013
    • (2008) Brief Bioinform , vol.9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 40
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository and associated resources
    • PID: 18931379
    • Kiefer F, Arnold K, Künzli M, Bordoli L, Schwede T (2009) The SWISS-MODEL Repository and associated resources. Nucleic Acids Res 37:D387–D392. doi:10.1093/nar/gkn750
    • (2009) Nucleic Acids Res , vol.37 , pp. D387-D392
    • Kiefer, F.1    Arnold, K.2    Künzli, M.3    Bordoli, L.4    Schwede, T.5
  • 41
    • 42149088826 scopus 로고    scopus 로고
    • Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
    • PID: 18340444
    • Kim M-S, Lei X (2008) Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR. Appl Microbiol Biotechnol 79:69–75. doi:10.1007/s00253-008-1412-7
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 69-75
    • Kim, M.-S.1    Lei, X.2
  • 42
    • 0035027846 scopus 로고    scopus 로고
    • Biological control of fungal strawberry diseases by Serratia plymuthica HRO-C48
    • Kurze S, Bahl H, Dahl R, Berg G (2001) Biological control of fungal strawberry diseases by Serratia plymuthica HRO-C48. Plant Dis 85:529–534. doi:10.1094/pdis.2001.85.5.529
    • (2001) Plant Dis , vol.85 , pp. 529-534
    • Kurze, S.1    Bahl, H.2    Dahl, R.3    Berg, G.4
  • 43
    • 56649096020 scopus 로고    scopus 로고
    • Genome data mining for everyone
    • PID: 19017486
    • Lee GW, Kim S (2008) Genome data mining for everyone. BMB Rep 41:757–764. doi:10.5483/BMBRep.2008.41.11.757
    • (2008) BMB Rep , vol.41 , pp. 757-764
    • Lee, G.W.1    Kim, S.2
  • 44
    • 38049029832 scopus 로고    scopus 로고
    • Data Mining in Genomics
    • PID: 18194724
    • Lee JK, Williams PD, Cheon S (2008) Data Mining in Genomics. Clin Lab Med 28:145–166. doi:10.1016/j.cll.2007.10.010
    • (2008) Clin Lab Med , vol.28 , pp. 145-166
    • Lee, J.K.1    Williams, P.D.2    Cheon, S.3
  • 45
    • 0033963277 scopus 로고    scopus 로고
    • From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase
    • PID: 10679530
    • Lehmann M, Kostrewa D, Wyss M, Brugger R, D’Arcy A, Pasamontes L, van Loon APGM (2000) From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. Protein Eng 13:49–57. doi:10.1093/protein/13.1.49
    • (2000) Protein Eng , vol.13 , pp. 49-57
    • Lehmann, M.1    Kostrewa, D.2    Wyss, M.3    Brugger, R.4    D’Arcy, A.5    Pasamontes, L.6    van Loon, A.P.G.M.7
  • 47
    • 0345393313 scopus 로고    scopus 로고
    • Phytase enzymology, applications, and biotechnology
    • PID: 14677699
    • Lei X-G, Porres JM (2003) Phytase enzymology, applications, and biotechnology. Biotechnol Lett 25:1787–1794. doi:10.1023/A:1026224101580
    • (2003) Biotechnol Lett , vol.25 , pp. 1787-1794
    • Lei, X.-G.1    Porres, J.M.2
  • 49
    • 57649155502 scopus 로고    scopus 로고
    • Molecular cloning, characterization, and expression of the phytase gene from marine yeast Kodamaea ohmeri BG3
    • PID: 18672057
    • Li X, Liu Z, Chi Z, Li J, Wang X (2009) Molecular cloning, characterization, and expression of the phytase gene from marine yeast Kodamaea ohmeri BG3. Mycol Res 113:24–32. doi:10.1016/j.mycres.2008.07.003
    • (2009) Mycol Res , vol.113 , pp. 24-32
    • Li, X.1    Liu, Z.2    Chi, Z.3    Li, J.4    Wang, X.5
  • 50
    • 84885181285 scopus 로고    scopus 로고
    • Site-directed mutagenesis improves the thermostability and catalytic efficiency of Aspergillus niger N25 phytase mutated by I44E and T252R
    • PID: 23907680
    • Liao Y, Li C-M, Chen H, Wu Q, Shan Z, Han X-Y (2013) Site-directed mutagenesis improves the thermostability and catalytic efficiency of Aspergillus niger N25 phytase mutated by I44E and T252R. Appl Biochem Biotechnol 171:900–915. doi:10.1007/s12010-013-0380-2
    • (2013) Appl Biochem Biotechnol , vol.171 , pp. 900-915
    • Liao, Y.1    Li, C.-M.2    Chen, H.3    Wu, Q.4    Shan, Z.5    Han, X.-Y.6
  • 51
    • 34547768136 scopus 로고    scopus 로고
    • Distribution and diversity of phytate-mineralizing bacteria
    • PID: 18043643
    • Lim BL, Yeung P, Cheng C, Hill JE (2007) Distribution and diversity of phytate-mineralizing bacteria. ISME J 1:321–330. doi:10.1038/ismej.2007.40
    • (2007) ISME J , vol.1 , pp. 321-330
    • Lim, B.L.1    Yeung, P.2    Cheng, C.3    Hill, J.E.4
  • 52
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • PID: 10655611
    • Lim D, Golovan S, Forsberg CW, Jia Z (2000) Crystal structures of Escherichia coli phytase and its complex with phytate. Nat Struct Biol 7:108–113. doi:10.1038/72371
    • (2000) Nat Struct Biol , vol.7 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 53
    • 34547743920 scopus 로고    scopus 로고
    • A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris
    • PID: 17657539
    • Luo H, Huang H, Yang P, Wang Y, Yuan T, Wu N, Yao B, Fan Y (2007) A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris. Curr Microbiol 55:185–192. doi:10.1007/s00284-006-0586-4
    • (2007) Curr Microbiol , vol.55 , pp. 185-192
    • Luo, H.1    Huang, H.2    Yang, P.3    Wang, Y.4    Yuan, T.5    Wu, N.6    Yao, B.7    Fan, Y.8
  • 55
    • 78650678024 scopus 로고    scopus 로고
    • Assessment of gastrointestinal pH, fluid and lymphoid tissue in the guinea pig, rabbit and pig, and implications for their use in drug development
    • PID: 20932902
    • Merchant HA, McConnell EL, Liu F, Ramaswamy C, Kulkarni RP, Basit AW, Murdan S (2011) Assessment of gastrointestinal pH, fluid and lymphoid tissue in the guinea pig, rabbit and pig, and implications for their use in drug development. Eur J Pharm Sci 42:3–10. doi:10.1016/j.ejps.2010.09.019
    • (2011) Eur J Pharm Sci , vol.42 , pp. 3-10
    • Merchant, H.A.1    McConnell, E.L.2    Liu, F.3    Ramaswamy, C.4    Kulkarni, R.P.5    Basit, A.W.6    Murdan, S.7
  • 56
    • 84882570279 scopus 로고    scopus 로고
    • Effect of diet grinding and pelleting fed either dry or liquid feed on dry matter and pH in the stomach of pigs and the development of gastric ulcers
    • Moesseler A, Wintermann M, Sander SJ, Kamphues J (2012) Effect of diet grinding and pelleting fed either dry or liquid feed on dry matter and pH in the stomach of pigs and the development of gastric ulcers. J Anim Sci 90:343–345. doi:10.2527/jas.53772
    • (2012) J Anim Sci , vol.90 , pp. 343-345
    • Moesseler, A.1    Wintermann, M.2    Sander, S.J.3    Kamphues, J.4
  • 58
    • 0345257904 scopus 로고    scopus 로고
    • The term phytase comprises several different classes of enzymes
    • PID: 14630039
    • Mullaney EJ, Ullah AH (2003) The term phytase comprises several different classes of enzymes. Biochem Biophys Res Commun 312:179–184. doi:10.1016/j.bbrc.2003.09.176
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 179-184
    • Mullaney, E.J.1    Ullah, A.H.2
  • 60
    • 84924801732 scopus 로고    scopus 로고
    • Molecular and biochemical characteristics of beta-propeller phytase from marine Pseudomonas sp. BS10-3 and its potential application for animal feed additives
    • PID: 25112322
    • Nam S-J, Kim Y-O, Ko T-K, Kang J-K, Chun K-H, Auh J-H, Lee I-K, Park S, Oh BC (2014) Molecular and biochemical characteristics of beta-propeller phytase from marine Pseudomonas sp. BS10-3 and its potential application for animal feed additives. J Microbiol Biotechnol 24:1413–1420. doi:10.4014/jmb.1407.07063
    • (2014) J Microbiol Biotechnol , vol.24 , pp. 1413-1420
    • Nam, S.-J.1    Kim, Y.-O.2    Ko, T.-K.3    Kang, J.-K.4    Chun, K.-H.5    Auh, J.-H.6    Lee, I.-K.7    Park, S.8    Oh, B.C.9
  • 61
    • 84976249562 scopus 로고
    • A research of the effect of the combined feeds with different participation of calcium and phosphorus for growing pigs
    • Nedeva R, Knev M (1993) A research of the effect of the combined feeds with different participation of calcium and phosphorus for growing pigs. Zhivotnov"dni Nauk 30:61–66
    • (1993) Zhivotnov"dni Nauk , vol.30 , pp. 61-66
    • Nedeva, R.1    Knev, M.2
  • 62
    • 79955720112 scopus 로고    scopus 로고
    • A thermostable phytase from Neosartorya spinosa BCC 41923 and its expression in Pichia pastoris
    • PID: 21538247
    • Pandee P, Summpunn P, Wiyakrutta S, Isarangkul D, Meevootisom V (2011) A thermostable phytase from Neosartorya spinosa BCC 41923 and its expression in Pichia pastoris. J Microbiol 49:257–264. doi:10.1007/s12275-011-0369-x
    • (2011) J Microbiol , vol.49 , pp. 257-264
    • Pandee, P.1    Summpunn, P.2    Wiyakrutta, S.3    Isarangkul, D.4    Meevootisom, V.5
  • 64
    • 84862697946 scopus 로고    scopus 로고
    • The PhyloPythiaS web server for taxonomic assignment of metagenome sequences
    • PID: 22745671
    • Patil KR, Roune L, McHardy AC (2012) The PhyloPythiaS web server for taxonomic assignment of metagenome sequences. PLoS One 7:e38581. doi:10.1371/journal.pone.0038581
    • (2012) PLoS One , vol.7 , pp. e38581
    • Patil, K.R.1    Roune, L.2    McHardy, A.C.3
  • 65
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • PID: 21959131
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8:785–786. doi:10.1038/nmeth.1701
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 67
    • 84924025921 scopus 로고    scopus 로고
    • Isolation and molecular characterization of thermostable phytase from Bacillus subtilis (BSPhyARRMK33)
    • PID: 25588529
    • Reddy CS, Achary VMM, Manna M, Singh J, Kaul T, Reddy MK (2015) Isolation and molecular characterization of thermostable phytase from Bacillus subtilis (BSPhyARRMK33). Appl Biochem Biotechnol 175:3058–3067. doi:10.1007/s12010-015-1487-4
    • (2015) Appl Biochem Biotechnol , vol.175 , pp. 3058-3067
    • Reddy, C.S.1    Achary, V.M.M.2    Manna, M.3    Singh, J.4    Kaul, T.5    Reddy, M.K.6
  • 68
    • 3843148288 scopus 로고    scopus 로고
    • Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1
    • PID: 14727093
    • Sajidan A, Farouk A, Greiner R, Jungblut P, Müller E-C, Borriss R (2004) Molecular and physiological characterisation of a 3-phytase from soil bacterium Klebsiella sp. ASR1. Appl Microbiol Biotechnol 65:110–118. doi:10.1007/s00253-003-1530-1
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 110-118
    • Sajidan, A.1    Farouk, A.2    Greiner, R.3    Jungblut, P.4    Müller, E.-C.5    Borriss, R.6
  • 70
    • 84857737663 scopus 로고    scopus 로고
    • Reversible and irreversible denaturation processes in globular proteins: from collective to molecular spectroscopic analysis
    • Sassi P, Perticaroli S, Comez L, Lupi L, Paolantoni M, Fioretto D, Morresi A (2012) Reversible and irreversible denaturation processes in globular proteins: from collective to molecular spectroscopic analysis. J Raman Spectrosc 43:273–279. doi:10.1002/jrs.3013
    • (2012) J Raman Spectrosc , vol.43 , pp. 273-279
    • Sassi, P.1    Perticaroli, S.2    Comez, L.3    Lupi, L.4    Paolantoni, M.5    Fioretto, D.6    Morresi, A.7
  • 71
    • 37549069355 scopus 로고    scopus 로고
    • Phytate-degrading enzymes in pig nutrition
    • Selle PH, Ravindran V (2008) Phytate-degrading enzymes in pig nutrition. Livestock Sci 113:99–122. doi:10.1016/j.livsci.2007.05.014
    • (2008) Livestock Sci , vol.113 , pp. 99-122
    • Selle, P.H.1    Ravindran, V.2
  • 72
    • 50249106225 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a new phytase from the phytopathogenic bacterium Pectobacterium wasabiae DSMZ 18074
    • PID: 18667849
    • Shao N, Huang H, Meng K, Luo H, Wang Y, Yang P, Yao B (2008) Cloning, expression, and characterization of a new phytase from the phytopathogenic bacterium Pectobacterium wasabiae DSMZ 18074. J Microbiol Biotechnol 18:1221–1226
    • (2008) J Microbiol Biotechnol , vol.18 , pp. 1221-1226
    • Shao, N.1    Huang, H.2    Meng, K.3    Luo, H.4    Wang, Y.5    Yang, P.6    Yao, B.7
  • 73
    • 40649106915 scopus 로고    scopus 로고
    • A novel phytase gene appA from Buttiauxella sp. GC21 isolated from grass carp intestine
    • Shi P, Huang H, Wang Y, Luo H, Wu B, Meng K, Yang P, Yao B (2008) A novel phytase gene appA from Buttiauxella sp. GC21 isolated from grass carp intestine. Aquaculture 275:70–75. doi:10.1016/j.aquaculture.2008.01.021
    • (2008) Aquaculture , vol.275 , pp. 70-75
    • Shi, P.1    Huang, H.2    Wang, Y.3    Luo, H.4    Wu, B.5    Meng, K.6    Yang, P.7    Yao, B.8
  • 74
    • 84890854387 scopus 로고    scopus 로고
    • Multi-site saturation by OmniChange yields a pH- and thermally improved phytase
    • PID: 24315971
    • Shivange AV, Dennig A, Schwaneberg U (2014) Multi-site saturation by OmniChange yields a pH- and thermally improved phytase. J Biotechnol 170:68–72. doi:10.1016/j.jbiotec.2013.11.014
    • (2014) J Biotechnol , vol.170 , pp. 68-72
    • Shivange, A.V.1    Dennig, A.2    Schwaneberg, U.3
  • 76
    • 57449117452 scopus 로고    scopus 로고
    • Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile
    • PID: 19054669
    • Singh B, Satyanarayana T (2009) Characterization of a HAP-phytase from a thermophilic mould Sporotrichum thermophile. Bioresour Technol 100:2046–2051. doi:10.1016/j.biortech.2008.10.025
    • (2009) Bioresour Technol , vol.100 , pp. 2046-2051
    • Singh, B.1    Satyanarayana, T.2
  • 77
    • 80051765336 scopus 로고    scopus 로고
    • Recent advances in research on enzymes for poultry diets
    • Slominski BA (2011) Recent advances in research on enzymes for poultry diets. Poultry Sci 90:2013–2023. doi:10.3382/ps.2011-01372
    • (2011) Poultry Sci , vol.90 , pp. 2013-2023
    • Slominski, B.A.1
  • 78
    • 0030965606 scopus 로고    scopus 로고
    • Roles of disulfide bonds in bacterial alkaline phosphatase
    • PID: 9045630
    • Sone M, Kishigami S, Yoshihisa T, Ito K (1997) Roles of disulfide bonds in bacterial alkaline phosphatase. J Biol Chem 272:6174–6178. doi:10.1074/jbc.272.10.6174
    • (1997) J Biol Chem , vol.272 , pp. 6174-6178
    • Sone, M.1    Kishigami, S.2    Yoshihisa, T.3    Ito, K.4
  • 79
    • 84880364412 scopus 로고    scopus 로고
    • Long-term phosphorus fertilisation increased the diversity of the total bacterial community and the phoD phosphorus mineraliser group in pasture soils
    • Tan H, Barret M, Mooij MJ, Rice O, Morrissey JP, Dobson AD, Griffiths BS, O’Gara F (2013) Long-term phosphorus fertilisation increased the diversity of the total bacterial community and the phoD phosphorus mineraliser group in pasture soils. Biol Fertil Soils 49:661–672. doi:10.1007/s00374-012-0755-5
    • (2013) Biol Fertil Soils , vol.49 , pp. 661-672
    • Tan, H.1    Barret, M.2    Mooij, M.J.3    Rice, O.4    Morrissey, J.P.5    Dobson, A.D.6    Griffiths, B.S.7    O’Gara, F.8
  • 80
    • 79951576528 scopus 로고    scopus 로고
    • Semi-rational site-directed mutagenesis of phyI1s from Aspergillus niger 113 at two residue to improve its phytase activity
    • PID: 20526743
    • Tian YS, Peng RH, Xu J, Zhao W, Gao F, Fu XY, Xiong AS, Yao QH (2011) Semi-rational site-directed mutagenesis of phyI1s from Aspergillus niger 113 at two residue to improve its phytase activity. Mol Biol Rep 38:977–982. doi:10.1007/s11033-010-0192-1
    • (2011) Mol Biol Rep , vol.38 , pp. 977-982
    • Tian, Y.S.1    Peng, R.H.2    Xu, J.3    Zhao, W.4    Gao, F.5    Fu, X.Y.6    Xiong, A.S.7    Yao, Q.H.8
  • 81
    • 4744372269 scopus 로고    scopus 로고
    • Effects of a novel disulfide bond and engineered electrostatic interactions on the thermostability of azurin
    • PID: 15449946
    • Tigerstrom A, Schwarz F, Karlsson G, Okvist M, Alvarez-Rua C, Maeder D, Robb FT, Sjolin L (2004) Effects of a novel disulfide bond and engineered electrostatic interactions on the thermostability of azurin. Biochemistry 43:12563–12574. doi:10.1021/bi048926x
    • (2004) Biochemistry , vol.43 , pp. 12563-12574
    • Tigerstrom, A.1    Schwarz, F.2    Karlsson, G.3    Okvist, M.4    Alvarez-Rua, C.5    Maeder, D.6    Robb, F.T.7    Sjolin, L.8
  • 82
    • 76849101050 scopus 로고    scopus 로고
    • A thermostable phytase from Bacillus sp. MD2: cloning, expression and high-level production in Escherichia coli
    • PID: 19997958
    • Tran TT, Mamo G, Mattiasson B, Hatti-Kaul R (2010) A thermostable phytase from Bacillus sp. MD2: cloning, expression and high-level production in Escherichia coli. J Ind Microbiol Biotechnol 37:279–287. doi:10.1007/s10295-009-0671-3
    • (2010) J Ind Microbiol Biotechnol , vol.37 , pp. 279-287
    • Tran, T.T.1    Mamo, G.2    Mattiasson, B.3    Hatti-Kaul, R.4
  • 83
    • 0036315591 scopus 로고    scopus 로고
    • Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis
    • PID: 12111145
    • Tye AJ, Siu FKY, Leung TYC, Lim BL (2002) Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis. Appl Microbiol Biotechnol 59:190–197. doi:10.1007/s00253-002-1033-5
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 190-197
    • Tye, A.J.1    Siu, F.K.Y.2    Leung, T.Y.C.3    Lim, B.L.4
  • 84
    • 0025915380 scopus 로고
    • Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase
    • PID: 1989985
    • Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL (1991) Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem 266:2313–2319
    • (1991) J Biol Chem , vol.266 , pp. 2313-2319
    • Van Etten, R.L.1    Davidson, R.2    Stevis, P.E.3    MacArthur, H.4    Moore, D.L.5
  • 86
    • 20044364585 scopus 로고    scopus 로고
    • Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem
    • PID: 15776271
    • Vats P, Banerjee UC (2005) Biochemical characterisation of extracellular phytase (myo-inositol hexakisphosphate phosphohydrolase) from a hyper-producing strain of Aspergillus niger van Teighem. J Ind Microbiol Biotechnol 32:141–147. doi:10.1007/s10295-005-0214-5
    • (2005) J Ind Microbiol Biotechnol , vol.32 , pp. 141-147
    • Vats, P.1    Banerjee, U.C.2
  • 87
    • 0033555677 scopus 로고    scopus 로고
    • A correlation between the loss of hydrophobic core packing interactions and protein stability
    • PID: 9878446
    • Vlassi M, Cesareni G, Kokkinidis M (1999) A correlation between the loss of hydrophobic core packing interactions and protein stability. J Mol Biol 285:817–827. doi:10.1006/jmbi.1998.2342
    • (1999) J Mol Biol , vol.285 , pp. 817-827
    • Vlassi, M.1    Cesareni, G.2    Kokkinidis, M.3
  • 88
    • 84896868441 scopus 로고    scopus 로고
    • Improving specific activity and thermostability of Escherichia coli phytase by structure-based rational design
    • PID: 24518264
    • Wu T-H, Chen C-C, Cheng Y-S, Ko T-P, Lin C-Y, Lai H-L, Huang T-Y, Liu J-R, Guo R-T (2014) Improving specific activity and thermostability of Escherichia coli phytase by structure-based rational design. J Biotechnol 175:1–6. doi:10.1016/j.jbiotec.2014.01.034
    • (2014) J Biotechnol , vol.175 , pp. 1-6
    • Wu, T.-H.1    Chen, C.-C.2    Cheng, Y.-S.3    Ko, T.-P.4    Lin, C.-Y.5    Lai, H.-L.6    Huang, T.-Y.7    Liu, J.-R.8    Guo, R.-T.9
  • 89
    • 2342501800 scopus 로고    scopus 로고
    • Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine
    • PID: 15136045
    • Xiang T, Liu Q, Deacon AM, Koshy M, Kriksunov IA, Lei XG, Hao Q, Thiel DJ (2004) Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine. J Mol Biol 339:437–445. doi:10.1016/s0022-2836(04)00372-9
    • (2004) J Mol Biol , vol.339 , pp. 437-445
    • Xiang, T.1    Liu, Q.2    Deacon, A.M.3    Koshy, M.4    Kriksunov, I.A.5    Lei, X.G.6    Hao, Q.7    Thiel, D.J.8
  • 90
    • 84884820996 scopus 로고    scopus 로고
    • Improving the thermostability of Escherichia coli phytase, appA, by enhancement of glycosylation
    • PID: 23794051
    • Yao MZ, Wang X, Wang W, Fu YJ, Liang AH (2013) Improving the thermostability of Escherichia coli phytase, appA, by enhancement of glycosylation. Biotechnol Lett 35:1669–1676. doi:10.1007/s10529-013-1255-x
    • (2013) Biotechnol Lett , vol.35 , pp. 1669-1676
    • Yao, M.Z.1    Wang, X.2    Wang, W.3    Fu, Y.J.4    Liang, A.H.5
  • 91
    • 83555177202 scopus 로고    scopus 로고
    • Phytases: crystal structures, protein engineering and potential biotechnological applications
    • PID: 22017627
    • Yao MZ, Zhang YH, Lu WL, Hu MQ, Wang W, Liang AH (2012) Phytases: crystal structures, protein engineering and potential biotechnological applications. J Appl Microbiol 112:1–14. doi:10.1111/j.1365-2672.2011.05181.x
    • (2012) J Appl Microbiol , vol.112 , pp. 1-14
    • Yao, M.Z.1    Zhang, Y.H.2    Lu, W.L.3    Hu, M.Q.4    Wang, W.5    Liang, A.H.6
  • 92
    • 84884603827 scopus 로고    scopus 로고
    • Purification and characterization of a novel neutral and heat-tolerant phytase from a newly isolated strain Bacillus nealsonii ZJ0702
    • PID: 24073799
    • Yu P, Chen Y (2013) Purification and characterization of a novel neutral and heat-tolerant phytase from a newly isolated strain Bacillus nealsonii ZJ0702. BMC Biotechnol 13:78–84. doi:10.1186/1472-6750-13-78
    • (2013) BMC Biotechnol , vol.13 , pp. 78-84
    • Yu, P.1    Chen, Y.2
  • 93
    • 76749170185 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a novel phytase with low pH optimum and strong proteolysis resistance from Aspergillus ficuum NTG-23
    • PID: 20144543
    • Zhang GQ, Dong XF, Wang ZH, Zhang Q, Wang HX, Tong JM (2010) Purification, characterization, and cloning of a novel phytase with low pH optimum and strong proteolysis resistance from Aspergillus ficuum NTG-23. Bioresour Technol 101:4125–4131. doi:10.1016/j.biortech.2010.01.001
    • (2010) Bioresour Technol , vol.101 , pp. 4125-4131
    • Zhang, G.Q.1    Dong, X.F.2    Wang, Z.H.3    Zhang, Q.4    Wang, H.X.5    Tong, J.M.6
  • 94
    • 4444292893 scopus 로고    scopus 로고
    • Properties of A. ficuum AS3.324 phytase expressed in tobacco
    • Zhang LH, An LJ, Gao XR, Wang YJ (2005) Properties of A. ficuum AS3.324 phytase expressed in tobacco. Process Biochem 40:213–216. doi:10.1016/j.procbio.2003.12.005
    • (2005) Process Biochem , vol.40 , pp. 213-216
    • Zhang, L.H.1    An, L.J.2    Gao, X.R.3    Wang, Y.J.4
  • 95
    • 82455168003 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a new alkaline β-propeller phytase from the insect symbiotic bacterium Janthinobacterium sp. TN115
    • PID: 21562981
    • Zhang R, Yang P, Huang H, Yuan T, Shi P, Meng K, Yao B (2011) Molecular and biochemical characterization of a new alkaline β-propeller phytase from the insect symbiotic bacterium Janthinobacterium sp. TN115. Appl Microbiol Biotechnol 92:317–325. doi:10.1007/s00253-011-3309-0
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 317-325
    • Zhang, R.1    Yang, P.2    Huang, H.3    Yuan, T.4    Shi, P.5    Meng, K.6    Yao, B.7
  • 96
    • 34248192717 scopus 로고    scopus 로고
    • Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase
    • PID: 17351092
    • Zhang WM, Mullaney EJ, Lei XG (2007) Adopting selected hydrogen bonding and ionic interactions from Aspergillus fumigatus phytase structure improves the thermostability of Aspergillus niger PhyA phytase. Appl Environ Microbiol 73:3069–3076. doi:10.1128/aem.02970-06
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3069-3076
    • Zhang, W.M.1    Mullaney, E.J.2    Lei, X.G.3
  • 97
    • 78449254843 scopus 로고    scopus 로고
    • Engineering of protease-resistant phytase from Penicillium sp.: High thermal stability, low optimal temperature and pH
    • PID: 20826112
    • Zhao QQ, Liu HL, Zhang Y, Zhang YZ (2010) Engineering of protease-resistant phytase from Penicillium sp.: High thermal stability, low optimal temperature and pH. J Biosci Bioeng 110:638–645. doi:10.1016/j.jbiosc.2010.08.003
    • (2010) J Biosci Bioeng , vol.110 , pp. 638-645
    • Zhao, Q.Q.1    Liu, H.L.2    Zhang, Y.3    Zhang, Y.Z.4
  • 98
    • 85027921848 scopus 로고    scopus 로고
    • Modifying thermostability of AppA from Escherichia coli
    • PID: 20213104
    • Zhu WH, Qiao DR, Huang M, Yang G, Xu H, Cao Y (2010) Modifying thermostability of AppA from Escherichia coli. Curr Microbiol 61:267–273. doi:10.1007/s00284-010-9606-5
    • (2010) Curr Microbiol , vol.61 , pp. 267-273
    • Zhu, W.H.1    Qiao, D.R.2    Huang, M.3    Yang, G.4    Xu, H.5    Cao, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.