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Volumn 27, Issue 8, 2010, Pages 747-754

Transglutaminase: New insights into gelatin nanoparticle cross-linking

Author keywords

Cross linking; Drug delivery; Gelatin; Nanoparticle; Stability

Indexed keywords

GELATIN; GELATIN NANOPARTICLE; NANOPARTICLE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 78049461954     PISSN: 02652048     EISSN: 14645246     Source Type: Journal    
DOI: 10.3109/02652048.2010.518773     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 78049483727 scopus 로고    scopus 로고
    • Protein nanoparticles for drug delivery
    • Japan. 2006-JP325987 2007072982 WO 20070628
    • Aimi M, Nemori R, Kojima M, Kishima M. 2006. Protein nanoparticles for drug delivery. Fujifilm Corporation, Japan. 2006-JP325987[2007072982], WO 20070628.
    • (2006) Fujifilm Corporation
    • Aimi, M.1    Nemori, R.2    Kojima, M.3    Kishima, M.4
  • 2
    • 78049456631 scopus 로고    scopus 로고
    • Enzymatically crosslinked protein nanoparticles
    • Japan. 2007- JP51856 2007086613
    • Aimi M, Nemori R, Miyashita Y, Yokoyama H. 2007. Enzymatically crosslinked protein nanoparticles. Fujifilm Corporation, Japan. 2007- JP51856[2007086613], 26, 20070802.
    • (2007) Fujifilm Corporation , Issue.26 , pp. 20070802
    • Aimi, M.1    Nemori, R.2    Miyashita, Y.3    Yokoyama, H.4
  • 3
    • 58149479586 scopus 로고    scopus 로고
    • Effects of transglutaminase-induced cross-linking on properties of fish gelatin-nanoclay composite film
    • Bae HJ, Darby D, Kimmel R, Park HJ, Whiteside W. Effects of transglutaminase- induced cross-linking on properties of fish gelatin-nanoclay composite film. Food Chem, 2009;114 (1):180-9.
    • (2009) Food. Chem. , vol.114 , Issue.1 , pp. 180-189
    • Bae, H.J.1    Darby, D.2    Kimmel, R.3    Park, H.J.4    Whiteside, W.5
  • 4
    • 0035075477 scopus 로고    scopus 로고
    • Toxicological medical and industrial hygiene aspects of glutaraldehyde with particular reference to its biocidal use in cold sterilization procedures
    • Ballantyne B, Jordan SL. Toxicological, medical, and industrial hygiene aspects of glutaraldehyde with particular reference to its biocidal use in cold sterilization procedures. J Appl Toxicol, 2001;21 (2):131-51.
    • (2001) J. Appl. Toxicol. , vol.21 , Issue.2 , pp. 131-151
    • Ballantyne, B.1    Jordan, S.L.2
  • 5
    • 33845980609 scopus 로고    scopus 로고
    • Enzymatic cross-linking versus radical polymerization in the preparation of gelatin polyHIPEs and their performance as scaffolds in the culture of hepatocytes
    • Barbetta A, Massimi M, Devirgiliis LC, Dentini M. Enzymatic cross-linking versus radical polymerization in the preparation of gelatin polyHIPEs and their performance as scaffolds in the culture of hepatocytes.Biomacromolecules, 2006;7 (11):3059-68.
    • (2006) Biomacromolecules , vol.7 , Issue.11 , pp. 3059-3068
    • Barbetta, A.1    Massimi, M.2    Devirgiliis, L.C.3    Dentini, M.4
  • 6
    • 33745564300 scopus 로고    scopus 로고
    • Transglutaminase reactivity with gelatine: Perspective applications in tissue engineering
    • Bertoni F, Barbani N, Giusti P, Ciardelli G. Transglutaminase reactivity with gelatine: Perspective applications in tissue engineering. Biotechnol Lett, 2006;28 (10):697-702.
    • (2006) Biotechnol. Lett. , vol.28 , Issue.10 , pp. 697-702
    • Bertoni, F.1    Barbani, N.2    Giusti, P.3    Ciardelli, G.4
  • 7
    • 70349646446 scopus 로고    scopus 로고
    • Enzymatically catalyzed HES conjugation using microbial transglutaminase: Proof of feasibility
    • Besheer A, Hertel TC, Kressler J, Maeder K, Pietzsch M. Enzymatically catalyzed HES conjugation using microbial transglutaminase: Proof of feasibility. J Pharm Sci, 2009;98 (11):4420-8.
    • (2009) J. Pharm. Sci. , vol.98 , Issue.11 , pp. 4420-4428
    • Besheer, A.1    Hertel, T.C.2    Kressler, J.3    Maeder, K.4    Pietzsch, M.5
  • 8
    • 34548673743 scopus 로고    scopus 로고
    • Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties
    • Boenisch MP, Huss M, Weitl K, Kulozik U. Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. Int Dairy J, 2007;17 (11):1360-71.
    • (2007) Int. Dairy. J. , vol.17 , Issue.11 , pp. 1360-1371
    • Boenisch, M.P.1    Huss, M.2    Weitl, K.3    Kulozik, U.4
  • 12
    • 1842602725 scopus 로고    scopus 로고
    • Development of a new carrier system for oligonucleotides and plasmids based on gelatin nanoparticles
    • Coester C. Development of a new carrier system for oligonucleotides and plasmids based on gelatin nanoparticles. New Drugs, 2003;1: 14-17.
    • (2003) New Drugs , vol.1 , pp. 14-17
    • Coester, C.1
  • 13
    • 0034092776 scopus 로고    scopus 로고
    • Gelatin nanoparticles by two step desolvation-a new preparation method surface modifications and cell uptake
    • Coester CJ, Langer K, Von Briesen H, Kreuter J. Gelatin nanoparticles by two step desolvation-a new preparation method, surface modifications and cell uptake. J Microencapsul, 2000;17 (2):187-93.
    • (2000) J. Microencapsul. , vol.17 , Issue.2 , pp. 187-193
    • Coester, C.J.1    Langer, K.2    Von Briesen, H.3    Kreuter, J.4
  • 14
    • 62949217561 scopus 로고    scopus 로고
    • Transglutaminase 2 cross-linking of matrix proteins: Biological significance and medical applications
    • Collighan RJ, Griffin M. Transglutaminase 2 cross-linking of matrix proteins: Biological significance and medical applications. Amino Acids, 2009;36 (4):659-70.
    • (2009) Amino Acids , vol.36 , Issue.4 , pp. 659-670
    • Collighan, R.J.1    Griffin, M.2
  • 15
    • 46849096054 scopus 로고    scopus 로고
    • Stability and conformational changes of transglutaminase from streptomyces hygroscopicus in ethanol-aqueous medium
    • (Amsterdam The Netherlands)
    • Cui L, Du G, Zhang D, Fan X, Chen J. Stability and conformational changes of transglutaminase from Streptomyces hygroscopicus in ethanol-aqueous medium. Process Biochem, (Amsterdam, The Netherlands), 2008;43 (8):887-91.
    • (2008) Process Biochem , vol.43 , Issue.8 , pp. 887-891
    • Cui, L.1    Du, G.2    Zhang, D.3    Fan, X.4    Chen, J.5
  • 16
    • 3042541063 scopus 로고    scopus 로고
    • Characterization of gelatin based films modified with transglutaminase glyoxal and formaldehyde
    • de Carvalho RA, Grosso CRF. Characterization of gelatin based films modified with transglutaminase, glyoxal and formaldehyde. Food Hydrocoll, 2004;18 (5):717-26.
    • (2004) Food. Hydrocoll. , vol.18 , Issue.5 , pp. 717-726
    • De Carvalho, R.A.1    Grosso, C.R.F.2
  • 17
    • 0014010928 scopus 로고
    • Transglutaminase: Mechanistic features of the active site as determined by kinetic and inhibitor studies
    • Folk JE, Cole PW. Transglutaminase: Mechanistic features of the active site as determined by kinetic and inhibitor studies. Biochim Biophys Acta, 1966;122:244-64.
    • (1966) Biochim. Biophys. Acta. , vol.122 , pp. 244-264
    • Folk, J.E.1    Cole, P.W.2
  • 18
    • 1842581651 scopus 로고    scopus 로고
    • Asymmetrical flow field-flow fractionation and multiangle light scattering for analysis of gelatin nanoparticle drug carrier systems
    • Fraunhofer W, Winter G, Coester C. Asymmetrical flow field-flow fractionation and multiangle light scattering for analysis of gelatin nanoparticle drug carrier systems. Anal Chem, 2004;76 (7):1909-20.
    • (2004) Anal. Chem. , vol.76 , Issue.7 , pp. 1909-1920
    • Fraunhofer, W.1    Winter, G.2    Coester, C.3
  • 19
    • 77951488598 scopus 로고    scopus 로고
    • Ultrasonic resonator technology as a new quality control method evaluating gelatin nanoparticles
    • Fuchs S, Winter G, Coester C. Ultrasonic resonator technology as a new quality control method evaluating gelatin nanoparticles. J Microencapsul, 2010;27 (3):242-52.
    • (2010) J. Microencapsul. , vol.27 , Issue.3 , pp. 242-252
    • Fuchs, S.1    Winter, G.2    Coester, C.3
  • 20
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Natures biological glues
    • Griffin M, Casadio R, Bergamini CM. Transglutaminases: Natures biological glues. Biochem J, 2002;368 (2):377-96.
    • (2002) Biochem. J. , vol.368 , Issue.2 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 21
    • 56449121365 scopus 로고    scopus 로고
    • Transglutaminase-induced caseinate gelation for the microencapsulation of probiotic cells
    • Heidebach T, Foerst P, Kulozik U. Transglutaminase-induced caseinate gelation for the microencapsulation of probiotic cells. Int Dairy J, 2008;19 (2):77-84.
    • (2008) Int. Dairy. J. , vol.19 , Issue.2 , pp. 77-84
    • Heidebach, T.1    Foerst, P.2    Kulozik, U.3
  • 22
    • 35348880320 scopus 로고    scopus 로고
    • Protein cross-linking with oxidative enzymes and transglutaminase effects in meat protein systems
    • Lantto R. Protein cross-linking with oxidative enzymes and transglutaminase. Effects in meat protein systems. VTT Publ, 2007;642:1-114.
    • (2007) VTT Publ. , vol.642 , pp. 1-114
    • Lantto, R.1
  • 23
    • 33947574735 scopus 로고    scopus 로고
    • Soluble expression of a pro-transglutaminase from Streptomyces mobaraensis in escherichia coli
    • Marx CK, Hertel TC, Pietzsch M. Soluble expression of a pro-transglutaminase from Streptomyces mobaraensis in Escherichia coli. Enzyme Microb Technol, 2007;40 (6):1543-50.
    • (2007) Enzyme. Microb. Technol. , vol.40 , Issue.6 , pp. 1543-1550
    • Marx, C.K.1    Hertel, T.C.2    Pietzsch, M.3
  • 24
    • 42749091455 scopus 로고    scopus 로고
    • Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli and partial characterization of the active enzyme
    • Marx CK, Hertel TC, Pietzsch M. Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli and partial characterization of the active enzyme. Enzyme Microb Technol, 2008;42 (7):568-75.
    • (2008) Enzyme. Microb. Technol. , vol.42 , Issue.7 , pp. 568-575
    • Marx, C.K.1    Hertel, T.C.2    Pietzsch, M.3
  • 25
    • 0018162354 scopus 로고
    • Human epidermal transglutaminase: Stimulation by trypsin organic solvents and chaotropic salts
    • Plishker MF, Thorpe JM, Goldsmith LA. Human epidermal transglutaminase: Stimulation by trypsin, organic solvents, and chaotropic salts. Arch Biochem Biophys, 1978;191 (1):49-58.
    • (1978) Arch. Biochem. Biophys. , vol.191 , Issue.1 , pp. 49-58
    • Plishker, M.F.1    Thorpe, J.M.2    Goldsmith, L.A.3
  • 26
    • 34249327294 scopus 로고    scopus 로고
    • Targeted pharmaceutical nanocarriers for cancer therapy and imaging
    • Torchilin VP. Targeted pharmaceutical nanocarriers for cancer therapy and imaging. AAPS J, 2007;9 (2):E128-47.
    • (2007) AAPS J. , vol.9 , Issue.2
    • Torchilin, V.P.1
  • 27
  • 28
    • 0033992170 scopus 로고    scopus 로고
    • Desolvation process and surface characterization of protein nanoparticles
    • Weber C, Coester C, Kreuter J, Langer K. Desolvation process and surface characterization of protein nanoparticles. Int J of Pharmaceuticals, 2000;194 (1):91-102.
    • (2000) Int. J. of Pharmaceuticals. , vol.194 , Issue.1 , pp. 91-102
    • Weber, C.1    Coester, C.2    Kreuter, J.3    Langer, K.4
  • 29
    • 0035917935 scopus 로고    scopus 로고
    • High-cell-density fermentation for production of L-Ncarbamoylase using an expression system based on the escherichia coli rhaBAD promoter
    • Wilms B, Hauck A, Reuss M, Syldatk C, Mattes R, Siemann M, Altenbuchner J. High-cell-density fermentation for production of L-Ncarbamoylase using an expression system based on the Escherichia coli rhaBAD promoter. Biotechnol Bioeng, 2001;73 (2):95-103.
    • (2001) Biotechnol. Bioeng. , vol.73 , Issue.2 , pp. 95-103
    • Wilms, B.1    Hauck, A.2    Reuss, M.3    Syldatk, C.4    Mattes, R.5    Siemann, M.6    Altenbuchner, J.7
  • 30
    • 13244263136 scopus 로고    scopus 로고
    • A comparison of the activities of three betagalactosidases in aqueous-organic solvent mixtures
    • Yoon JH, McKenzie D. A comparison of the activities of three betagalactosidases in aqueous-organic solvent mixtures. Enzyme Microb Technol, 2005;36 (4):439-46.
    • (2005) Enzyme. Microb. Technol. , vol.36 , Issue.4 , pp. 439-446
    • Yoon, J.H.1    McKenzie, D.2
  • 31
    • 51249102955 scopus 로고    scopus 로고
    • Novel applications for microbial transglutaminase beyond food processing
    • Zhu Y, Tramper J. Novel applications for microbial transglutaminase beyond food processing. Trends Biotechnol, 2008;26 (10):559-65.
    • (2008) Trends Biotechnol. , vol.26 , Issue.10 , pp. 559-565
    • Zhu, Y.1    Tramper, J.2
  • 32
    • 34347251585 scopus 로고    scopus 로고
    • Method for quantifying the PEGylation of gelatin nanoparticle drug carrier systems using asymmetrical flow field-flow fractionation and refractive index detection
    • Zillies JC, Zwiorek K, Winter G, Coester C. Method for quantifying the PEGylation of gelatin nanoparticle drug carrier systems using asymmetrical flow field-flow fractionation and refractive index detection. Anal Chem, 2007;79 (12):4574-80.
    • (2007) Anal. Chem. , vol.79 , Issue.12 , pp. 4574-4580
    • Zillies, J.C.1    Zwiorek, K.2    Winter, G.3    Coester, C.4
  • 34
    • 40549096768 scopus 로고    scopus 로고
    • Delivery by cationic gelatin nanoparticles strongly increases the immunostimulatory effects of CpG ligonucleotides
    • Zwiorek K, Bourquin C, Battiany J, Winter G, Endres S, Hartmann G, Coester C. Delivery by cationic gelatin nanoparticles strongly increases the immunostimulatory effects of CpG ligonucleotides. Pharm Res, 2008;25 (3):551-62.
    • (2008) Pharm. Res. , vol.25 , Issue.3 , pp. 551-562
    • Zwiorek, K.1    Bourquin, C.2    Battiany, J.3    Winter, G.4    Endres, S.5    Hartmann, G.6    Coester, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.