메뉴 건너뛰기




Volumn 77, Issue 5, 2008, Pages 1033-1040

Cumulative improvements of thermostability and pH-activity profile of Aspergillus niger PhyA phytase by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY; HYDROLYSIS; MUTAGENESIS; PH EFFECTS; PHOSPHORUS;

EID: 37249041070     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-007-1239-7     Document Type: Article
Times cited : (30)

References (36)
  • 3
    • 0000170741 scopus 로고
    • Thermal instability of ribulose-1,5-bisphosphate carboxylase/oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii
    • Chen Z, Hong S, Spreitzer RJ (1993) Thermal instability of ribulose-1,5-bisphosphate carboxylase/oxygenase from a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii. Plant Physiol 101:1189-1194
    • (1993) Plant Physiol , vol.101 , pp. 1189-1194
    • Chen, Z.1    Hong, S.2    Spreitzer, R.J.3
  • 4
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: An update
    • Cherry JR, Fidantsef AL (2003) Directed evolution of industrial enzymes: an update. Curr Opin Biotech 14:438-443
    • (2003) Curr Opin Biotech , vol.14 , pp. 438-443
    • Cherry, J.R.1    Fidantsef, A.L.2
  • 5
    • 0037900194 scopus 로고    scopus 로고
    • Hyperthermostabilization of Bacillus lichniformis a-amylase and modulation of its stability over a 50°C temperature range
    • Declerck N, Machius M, Joyet P, Wiegand G, Huber R, Gaillardin C (2003) Hyperthermostabilization of Bacillus lichniformis a-amylase and modulation of its stability over a 50°C temperature range. Protein Eng 16:287-293
    • (2003) Protein Eng , vol.16 , pp. 287-293
    • Declerck, N.1    MacHius, M.2    Joyet, P.3    Wiegand, G.4    Huber, R.5    Gaillardin, C.6
  • 7
    • 1542442162 scopus 로고    scopus 로고
    • Effectiveness of an experimental consensus phytase in improving dietary phytate-phosphorus utilization by weanling pigs
    • Gentile JM, Roneker KR, Crowe SE, Pond WG, Lei XG (2003) Effectiveness of an experimental consensus phytase in improving dietary phytate-phosphorus utilization by weanling pigs. J Anim Sci 81:2751-2757
    • (2003) J Anim Sci , vol.81 , pp. 2751-2757
    • Gentile, J.M.1    Roneker, K.R.2    Crowe, S.E.3    Pond, W.G.4    Lei, X.G.5
  • 8
    • 0344289519 scopus 로고    scopus 로고
    • Role of glycosylation in the functional expression of an Aspergillus niger phytase (PhyA) in Pichia pastoris
    • Han Y, Lei XG (1999) Role of glycosylation in the functional expression of an Aspergillus niger phytase (PhyA) in Pichia pastoris. Arch Biochem Biophys 364:83-90
    • (1999) Arch Biochem Biophys , vol.364 , pp. 83-90
    • Han, Y.1    Lei, X.G.2
  • 9
    • 0032923801 scopus 로고    scopus 로고
    • Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiae
    • Han Y, Wilson DB, Lei XG (1999) Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiae. Appl Environ Microbiol 65:1915-1918
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1915-1918
    • Han, Y.1    Wilson, D.B.2    Lei, X.G.3
  • 13
    • 0033591464 scopus 로고    scopus 로고
    • Crystal structure of Aspergillus niger pH2.5 acid phosphatase at 2.4Å resolution
    • Kostrewa D, Wyss M, D'Arcy A, van Loon APGM (1999) Crystal structure of Aspergillus niger pH2.5 acid phosphatase at 2.4Å resolution. J Mol Biol 288:965-974
    • (1999) J Mol Biol , vol.288 , pp. 965-974
    • Kostrewa, D.1    Wyss, M.2    D'Arcy, A.3    Loon Apgm, V.4
  • 14
    • 33746075234 scopus 로고    scopus 로고
    • Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance
    • Law GHE, Gandelman OA, Tisi LC, Lowe CR, Murray JAH (2006) Mutagenesis of solvent-exposed amino acids in Photinus pyralis luciferase improves thermostability and pH-tolerance. Biochem J 397:305-312
    • (2006) Biochem J , vol.397 , pp. 305-312
    • Law, G.H.E.1    Gandelman, O.A.2    Tisi, L.C.3    Lowe, C.R.4    Murray, J.A.H.5
  • 15
    • 0348047619 scopus 로고    scopus 로고
    • Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge
    • Leemhuis H, J.Rozeboom H, Dijkstra BW, Dijkhuizen L (2004) Improved thermostability of Bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge. Proteins 54:128-134
    • (2004) Proteins , vol.54 , pp. 128-134
    • Leemhuis, H.1    J.rozeboom, H.2    Dijkstra, B.W.3    Dijkhuizen, L.4
  • 16
    • 0034767777 scopus 로고    scopus 로고
    • Biotechnological development of effective phytases for mineral nutrition and environmental protection
    • Lei XG, Stahl CH (2001) Biotechnological development of effective phytases for mineral nutrition and environmental protection. Appl Microbiol Biotechnol 57:474-481
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 474-481
    • Lei, X.G.1    Stahl, C.H.2
  • 17
    • 0033952704 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli phytase and its complex with phytate
    • Lim D, Golovan S, Forsberg CW, Jia1 Z (2000) Crystal structures of Escherichia coli phytase and its complex with phytate. Nat Struct Biol 7:108-113
    • (2000) Nat Struct Biol , vol.7 , pp. 108-113
    • Lim, D.1    Golovan, S.2    Forsberg, C.W.3    Jia, Z.4
  • 18
    • 0033768934 scopus 로고    scopus 로고
    • Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability
    • Liu H-L, Doleyres Y, M.Coutinho P, Ford C, J.Reilly P (2000) Replacement and deletion mutations in the catalytic domain and belt region of Aspergillus awamori glucoamylase to enhance thermostability. Protein Eng 13:655-659
    • (2000) Protein Eng , vol.13 , pp. 655-659
    • Liu, H.-L.1    Doleyres, Y.2    M.coutinho, P.3    Ford, C.4    J.reilly, P.5
  • 19
    • 4444336413 scopus 로고    scopus 로고
    • Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics
    • Liu Q, Huang Q, Lei XG, Hao Q (2004) Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics. Structure 12:1575-1583
    • (2004) Structure , vol.12 , pp. 1575-1583
    • Liu, Q.1    Huang, Q.2    Lei, X.G.3    Hao, Q.4
  • 21
    • 32944455102 scopus 로고    scopus 로고
    • Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain
    • Mamdouh Ba, Bassem K, Xavier R, Richard H, Samir B (2006) Thermostability enhancement and change in starch hydrolysis profile of the maltohexaose-forming amylase of Bacillus stearothermophilus US100 strain. Biochem J 394:51-56
    • (2006) Biochem J , vol.394 , pp. 51-56
    • Ba, M.1    Bassem, K.2    Xavier, R.3    Richard, H.4    Samir, B.5
  • 22
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews BW, Nicholson H, Becktel W (1987) Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci U S A 84:6663-6667
    • (1987) Proc Natl Acad Sci U S a , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.3
  • 25
    • 0031406972 scopus 로고    scopus 로고
    • Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix
    • Nakamura S, Tanaka T, Yada R, Nakai S (1997) Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix. Protein Eng 10:1263-1269
    • (1997) Protein Eng , vol.10 , pp. 1263-1269
    • Nakamura, S.1    Tanaka, T.2    Yada, R.3    Nakai, S.4
  • 26
    • 34249844436 scopus 로고    scopus 로고
    • Distribution of supplemental Escherichia coli AppA2 phytase activity in digesta of various gastrointestinal segments of young pigs
    • Pagano AR, Roneker KR, Lei XG (2007) Distribution of supplemental Escherichia coli AppA2 phytase activity in digesta of various gastrointestinal segments of young pigs. J Anim Sci 85:1444-1452
    • (2007) J Anim Sci , vol.85 , pp. 1444-1452
    • Pagano, A.R.1    Roneker, K.R.2    Lei, X.G.3
  • 27
    • 17644419962 scopus 로고    scopus 로고
    • Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase
    • Santarossa G, Lafranconi PG, Alquati C, DeGioia L, Alberghina L, Fantucci P, Lotti M (2005) Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase. FEBS Lett 579:2383-2386
    • (2005) FEBS Lett , vol.579 , pp. 2383-2386
    • Santarossa, G.1    Lafranconi, P.G.2    Alquati, C.3    Degioia, L.4    Alberghina, L.5    Fantucci, P.6    Lotti, M.7
  • 28
    • 0034073503 scopus 로고    scopus 로고
    • Molecular determinants of xylose isomerase thermal stability and activity: Analysis of thermozymes by site-directed mutagenesis
    • Sriprapundh D, Vieille C, Zeikus JG (2000) Molecular determinants of xylose isomerase thermal stability and activity: analysis of thermozymes by site-directed mutagenesis. Protein Eng 13:259-265
    • (2000) Protein Eng , vol.13 , pp. 259-265
    • Sriprapundh, D.1    Vieille, C.2    Zeikus, J.G.3
  • 29
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer WPC (1994) DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc Natl Acad Sci U S A 91:10747-10751
    • (1994) Proc Natl Acad Sci U S a , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 30
    • 0023080759 scopus 로고
    • Extracellular phytase (E.C.3.1.3.8.) from Aspergillus ficuum NRRL3135: Purification and characterization
    • Ullah AHJ, Gibson DM (1987) Extracellular phytase (E.C.3.1.3.8.) from Aspergillus ficuum NRRL3135: purification and characterization. Prep Biochem 17:63-91
    • (1987) Prep Biochem , vol.17 , pp. 63-91
    • Ullah, A.H.J.1    Gibson, D.M.2
  • 31
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell S, Argos P (1997) Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol 269:631-643
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 32
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
    • Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y (1994) Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. Eur J Biochem 226:277-283
    • (1994) Eur J Biochem , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5
  • 34
    • 2342501800 scopus 로고    scopus 로고
    • Crystal structure of a heat-resilient phytase from Aspergillus fumigatus, carrying a phosphorylated histidine
    • 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
    • (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
  • 35
    • 33845302023 scopus 로고    scopus 로고
    • Supplemental dietary inulin affects the bioavailability of iron in corn and soybean meal to young pigs
    • Yasuda K, Roneker KR, Miller DD, Welch RM, Lei XG (2006) Supplemental dietary inulin affects the bioavailability of iron in corn and soybean meal to young pigs. J Nutr 136:3033-3038
    • (2006) J Nutr , vol.136 , pp. 3033-3038
    • Yasuda, K.1    Roneker, K.R.2    Miller, D.D.3    Welch, R.M.4    Lei, X.G.5
  • 36
    • 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
    • Zhang W, 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
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3069-3076
    • Zhang, W.1    Mullaney, E.J.2    Lei, X.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.