메뉴 건너뛰기




Volumn 99, Issue 9, 2008, Pages 3794-3800

Thermal stability and conformational changes of transglutaminase from a newly isolated Streptomyces hygroscopicus

Author keywords

Conformational changes; Microbial transglutaminase; Streptomyces hygroscopicus; Thermal stability

Indexed keywords

DIFFERENTIAL SCANNING CALORIMETRY; ELECTROPHORESIS; MATHEMATICAL MODELS; REACTION KINETICS; THERMODYNAMIC STABILITY;

EID: 43849090971     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2007.07.017     Document Type: Article
Times cited : (46)

References (26)
  • 1
    • 0028322985 scopus 로고
    • Transglutaminase: protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D., and Paulsson M. Transglutaminase: protein cross-linking enzymes in tissues and body fluids. Thromb. Haemostasis 71 (1994) 402-415
    • (1994) Thromb. Haemostasis , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 3
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • Back J.F., Oakenfull D., and Smith M.B. Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 18 (1979) 5191-5196
    • (1979) Biochemistry , vol.18 , pp. 5191-5196
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 4
    • 0037835963 scopus 로고    scopus 로고
    • Purification and Properties of a transglutaminase produced by a Bacillus circulans strain isolated from the Amazon environment
    • Barros S.L.H., Assmann F., and Zachia A.M.A. Purification and Properties of a transglutaminase produced by a Bacillus circulans strain isolated from the Amazon environment. Biotechnol. Appl. Biochem. 37 (2003) 295-299
    • (2003) Biotechnol. Appl. Biochem. , vol.37 , pp. 295-299
    • Barros, S.L.H.1    Assmann, F.2    Zachia, A.M.A.3
  • 5
    • 0344665625 scopus 로고    scopus 로고
    • Application of transglutaminase in the modification of wool textile
    • Cortez J., Bonner P.L.R., and Griffin M. Application of transglutaminase in the modification of wool textile. Enzyme Microb. Technol. 34 (2004) 64-72
    • (2004) Enzyme Microb. Technol. , vol.34 , pp. 64-72
    • Cortez, J.1    Bonner, P.L.R.2    Griffin, M.3
  • 6
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: stability and function in aqueous and organic solvents
    • Cowan D.A. Thermophilic proteins: stability and function in aqueous and organic solvents. Comp. Biochem. Physiol. A Physiol 118 (1997) 429-438
    • (1997) Comp. Biochem. Physiol. A Physiol , vol.118 , pp. 429-438
    • Cowan, D.A.1
  • 7
    • 33646114081 scopus 로고    scopus 로고
    • Stabilization of a new microbial transglutaminase from Streptomyces hygroscopicus WSH03 - 13 by spray drying
    • Cui L., Zhang D., Huang L., Liu H., Du G., and Chen J. Stabilization of a new microbial transglutaminase from Streptomyces hygroscopicus WSH03 - 13 by spray drying. Process Biochem. 41 (2006) 1427-1431
    • (2006) Process Biochem. , vol.41 , pp. 1427-1431
    • Cui, L.1    Zhang, D.2    Huang, L.3    Liu, H.4    Du, G.5    Chen, J.6
  • 8
    • 34447248556 scopus 로고    scopus 로고
    • Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus
    • doi:10.1016/j.foodchem.2007.04.020
    • Cui L., Du G., Zhang D., Liu H., and Chen J. Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus. Food Chem. (2007) doi:10.1016/j.foodchem.2007.04.020
    • (2007) Food Chem.
    • Cui, L.1    Du, G.2    Zhang, D.3    Liu, H.4    Chen, J.5
  • 9
    • 0020394274 scopus 로고
    • A correlation between protein thermostability and resistance to proteolysis
    • Daniel R.M. A correlation between protein thermostability and resistance to proteolysis. Biochem. J. 207 (1982) 641-644
    • (1982) Biochem. J. , vol.207 , pp. 641-644
    • Daniel, R.M.1
  • 10
    • 34247365327 scopus 로고    scopus 로고
    • Improvement of shrink-resistance and tensile strength of wool fabric treated with a novel microbial transglutaminase from Streptomyces hygroscopicus
    • Du G., Cui L., Zhu Y., and Chen J. Improvement of shrink-resistance and tensile strength of wool fabric treated with a novel microbial transglutaminase from Streptomyces hygroscopicus. Enzyme Microb. Technol. 40 (2007) 1753-1757
    • (2007) Enzyme Microb. Technol. , vol.40 , pp. 1753-1757
    • Du, G.1    Cui, L.2    Zhu, Y.3    Chen, J.4
  • 11
    • 76549212824 scopus 로고
    • The enzymatic formation of hydroxamic acids from glutamine
    • Grossowicz N., Wainfan E., Borek E., and Waelsch H. The enzymatic formation of hydroxamic acids from glutamine. J. Biol. Chem. 187 (1950) 111-125
    • (1950) J. Biol. Chem. , vol.187 , pp. 111-125
    • Grossowicz, N.1    Wainfan, E.2    Borek, E.3    Waelsch, H.4
  • 12
    • 0035252563 scopus 로고    scopus 로고
    • Stabilization of Penicillium occitanis cellulases by spray drying in the presence of maltodextrin
    • Hafedh B., Semia D.C., and Ali G. Stabilization of Penicillium occitanis cellulases by spray drying in the presence of maltodextrin. Enzyme Microb. Technol. 28 (2001) 253-258
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 253-258
    • Hafedh, B.1    Semia, D.C.2    Ali, G.3
  • 13
    • 0032820434 scopus 로고    scopus 로고
    • Enzyme immobilization via microbial transglutaminase: a method for the generation of stable sensing surfaces
    • Josten A., Meuse M., Spener F., and Haalck L. Enzyme immobilization via microbial transglutaminase: a method for the generation of stable sensing surfaces. J. Mol. Catal. B: Enzym. 7 (1999) 57-66
    • (1999) J. Mol. Catal. B: Enzym. , vol.7 , pp. 57-66
    • Josten, A.1    Meuse, M.2    Spener, F.3    Haalck, L.4
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural protein during the assembly of head of bacteriophage T4. Nature (London) 227 (1970) 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0024503110 scopus 로고
    • The kinetics and mechanism of shear inactivation of lipase from Candida cylindracea
    • Lee Y.K., and Choo C.L. The kinetics and mechanism of shear inactivation of lipase from Candida cylindracea. Biotechn. Bioeng. 33 (1989) 183-190
    • (1989) Biotechn. Bioeng. , vol.33 , pp. 183-190
    • Lee, Y.K.1    Choo, C.L.2
  • 16
    • 36849156983 scopus 로고
    • Sensitivity of circular dichroism to protein tertiary structure class
    • Manavalan P., and Johnson Jr. W.C. Sensitivity of circular dichroism to protein tertiary structure class. Nature 305 (1983) 831-832
    • (1983) Nature , vol.305 , pp. 831-832
    • Manavalan, P.1    Johnson Jr., W.C.2
  • 17
    • 33645456647 scopus 로고    scopus 로고
    • Structural changes of microbial transglutaminase during thermal and high-pressure treatment
    • Menéndez O.H., Rawel S.U., and Henle T. Structural changes of microbial transglutaminase during thermal and high-pressure treatment. J. Agric. Food Chem. 54 (2006) 1716-1721
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 1716-1721
    • Menéndez, O.H.1    Rawel, S.U.2    Henle, T.3
  • 18
    • 0001641542 scopus 로고
    • Trends in Japanese soy protein research
    • Motoki M., and Seguro K. Trends in Japanese soy protein research. Information 5 (1994) 308-313
    • (1994) Information , vol.5 , pp. 308-313
    • Motoki, M.1    Seguro, K.2
  • 19
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • Richard L., Remmele Jr. R.L., Nancy S.N., Subhashini S., and Wayne R.G. Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry. Pharm. Res. 15 (1998) 200-208
    • (1998) Pharm. Res. , vol.15 , pp. 200-208
    • Richard, L.1    Remmele Jr., R.L.2    Nancy, S.N.3    Subhashini, S.4    Wayne, R.G.5
  • 20
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods
    • Sreerama N., and Woody R.W. Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242 (1994) 497-507
    • (1994) J. Mol. Biol. , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 21
    • 85007729648 scopus 로고
    • Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans
    • Washizu K., Ando K., Koikeda S., Hirose S., Matsuura A., Akagi H., Motoki M., and Takeuchi K. Molecular cloning of the gene for microbial transglutaminase from Streptoverticillium and its expression in Streptomyces lividans. Biosci. Biotechnol. Biochem. 58 (1994) 82-87
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 82-87
    • Washizu, K.1    Ando, K.2    Koikeda, S.3    Hirose, S.4    Matsuura, A.5    Akagi, H.6    Motoki, M.7    Takeuchi, K.8
  • 22
    • 7444246821 scopus 로고    scopus 로고
    • Enhancement of microbial transglutaminase production by Streptoverticillium mobaraense: application of a two-stage agitation speed control strategy
    • Yan G.L., Du G.C., Li Y., and Chen J. Enhancement of microbial transglutaminase production by Streptoverticillium mobaraense: application of a two-stage agitation speed control strategy. Process Biochem. 40 (2005) 963-968
    • (2005) Process Biochem. , vol.40 , pp. 963-968
    • Yan, G.L.1    Du, G.C.2    Li, Y.3    Chen, J.4
  • 23
    • 0026903661 scopus 로고
    • Enzyme immobilization on ion exchangers by forming an enzyme coating with transglutaminase as a crosslinker
    • Yoshiro K., Erika O., and Masao M. Enzyme immobilization on ion exchangers by forming an enzyme coating with transglutaminase as a crosslinker. Biosci. Biotechnol. Biochem. 56 (1992) 1323-1324
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1323-1324
    • Yoshiro, K.1    Erika, O.2    Masao, M.3
  • 24
    • 0037009166 scopus 로고    scopus 로고
    • pH control strategy of batch microbial transglutaminase production with Streptoverticillium mobaraense
    • Zheng M.Y., Du G.C., and Chen J. pH control strategy of batch microbial transglutaminase production with Streptoverticillium mobaraense. Enzyme Microb. Technol. 31 (2002) 477-481
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 477-481
    • Zheng, M.Y.1    Du, G.C.2    Chen, J.3
  • 25
    • 0029608871 scopus 로고
    • Microbial transglutaminase: a review on its production and application in food processing
    • Zhu Y., Rinzema A., Tramper J., and Bol J. Microbial transglutaminase: a review on its production and application in food processing. Appl. Microbiol. Biotechnol. 44 (1995) 277-282
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 26
    • 0030570131 scopus 로고    scopus 로고
    • Medium design based on stoiciometric analysis of microbial transglutaminase production by Streptoverticillium mobaraense
    • Zhu Y., Rinzema A., Tramper J., and Bol J. Medium design based on stoiciometric analysis of microbial transglutaminase production by Streptoverticillium mobaraense. Biotechnol. Bioeng. 50 (1996) 291-298
    • (1996) Biotechnol. Bioeng. , vol.50 , pp. 291-298
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.