Stability Properties of Thermoresponsive Poly(N-Isopropylacrylamide)-Trypsin Conjugates

References

• Abchowski A., Davis F. F. “Preparation and properties of polyethylene glycol-trypsin adducts”. Biochim. Biophys. Acta 1979; 578: 41–46
   PubMedGoogle Scholar
• Batra R., Gupta M. N. “Enhancement of enzyme activity in aqueous-organic solvent mixtures”. Biotechnol. Lett 1994; 16: 1059–1064
   Web of Science ®Google Scholar
• Charles M., Coughlin R. W., Hasselberger F. X. “Soluble-insoluble enzyme catalysts”. Biotechnol. Bioengng 1974; 16: 1553–1556
   PubMed Web of Science ®Google Scholar
• Chen J. P., Lee J. J., Liu H. S. “Comparison of isoamylase immobilization to insoluble and temperature-sensitive reversibly soluble carriers”. Biotechnol. Techn 1997; 11: 109–112
   Google Scholar
• Chen J. P., Hoffman A. S. “Polymer-protein conjugate II. Affinity precipitation separation of human immunogammaglobulin by a poly(N-isopropylacrylamide)-protein A conjugate”. Biomaterials 1990; 11: 631–634
   PubMed Web of Science ®Google Scholar
• Chen G., Hoffman A. S. “Preparation and properties of thermoreversible, phase-separating enzyme-oligo(N-isopropylacrylamide) conjugates”. Bioconjugate Chem 1993; 4: 509–514
   PubMed Web of Science ®Google Scholar
• Chen G., Hoffman A. S. “Synthesis of carboxylated poly(NIPAAm) oligomers and their application to form thermo-reversible polymer-enzyme conjugates”. J. Biomater. Sci. Poly. Edn 1994; 4: 371–382
   Google Scholar
• Chen G., Hoffman A. S. “Graft copolymers that exhibit temperature-induced phase transition over a wide range of pH“. Nature 1995; 373: 49–52
   PubMed Web of Science ®Google Scholar
• Chen J. P., Hsu M. S. “Preparations and properties of temperature-sensitive poly(N-isopropylacrylamide)-chymotrypsin conjugates”. J. Mol. Catal. B: Enz 1997; 2: 233
   Google Scholar
• Cong L., Kaul R., Dissing U., Mattiasson B. “A model study on Eudragit and polyethyleneimine as soluble carriers of α-amylase for repeated hydrolysis of starch”. J. Biotechnol 1995; 42: 75–84
   Web of Science ®Google Scholar
• Erlanger B. F., Kokowsky N., Cohen W. “The preparation and properties of two new chromogenic substrates of trypsin”. Arch. Biochem. Biophys 1961; 95: 271–278
   PubMed Web of Science ®Google Scholar
• Fujii M., Taniguchi M. “Application of reversibly soluble polymers in bioprocessing”. Trends Biotechnol 1991; 9: 191–196
   PubMed Web of Science ®Google Scholar
• Fujishige S., Kubota K., Ando I. “Phase transition of aqueous solutions of poly(N-isopropylacrylaraide) and poly(N-sopropylmethacrylamide)”. J. Phys. Chem 1989; 93: 3311–3313
   Web of Science ®Google Scholar
• Galaev I. ‘Smart’ polymers in biotechnology and medicine”. Russian Chem. Rev 1995; 64: 471–489
   Google Scholar
• Galaev I. Y., Mattiasson B. “Affinity thermoprecipitation of trypsin using soybean trypsin inhibitor conjugated with a thermo-reactive polymer, poly(N-vinyl caprolactam)”. Biotechnol.-Techn 1992; 6: 353–358
   Web of Science ®Google Scholar
• Galaev I., Gupta M. N., Mattiasson B. “Use smart polymers for bioseparations”. Chemtech 1996; 19–25, (December)
   Google Scholar
• Guoqiang D., Batra R., Kaul R., Gupta M. N., Mattiasson B. “Alternative modes of precipitation of Eudragit S 100: a potential ligand carrier for affinity precipitation of proteins”. Bioseparation 1995; 5: 339–350
   Google Scholar
• Harris P. A., Karlstöm G., Tjemeld F. “Enzyme purification using temperature-induced phase formation”. Bioseparation 1991; 2: 237–246
   PubMedGoogle Scholar
• Heskins M., Guillet J. E. “Solution properties of poly(N-isopropylacrylamide)”. J Macromolec. Sci. Chem 1968; 2: 1441–1455
   Google Scholar
• Hoshino K., Taniguchi M., Netsu Y., Fujii M. “Repeated hydrolysis of starch using amylase immobilized on a reversibly soluble-insoluble polymer”. J. Chem. Eng. Jpn 1989; 22: 54–59
   Web of Science ®Google Scholar
• Inada Y., Takahashi K., Yoshimoto T., Ajima A., Matsushima A., Saito Y. “Application of polyethylene glycol-modified enzymes in biotechnological processes: organic solvent-soluble enzymes”. Trends Biotechnol 1986; 4: 190–194
   Web of Science ®Google Scholar
• Karube I., Nakamoto Y., Suzuki S. “Photocontrol of urease activity in spiropyran collagen membrane”. Biochem. Biophys. Acta 1976; 445: 774–779
   PubMedGoogle Scholar
• Kokufuta E., Shimizu N., Nakamura I. “Preparation of polyelectrolyte-coated pH-sensitive poly(styrene) microcapsules and their application to initiation-cessation control of an enzyme reaction”. Biotechnol. Bioengng 1988; 32: 289–294
   PubMed Web of Science ®Google Scholar
• Kumar A., Galaev I. Yu., Mattiasson B. “Isolation and separation of α-amylase inhibitor from wheat meal by metal chelate affinity binding using Cu(II)-loaded copolymers of 1-vinylimidazole with N-isoproylacrylamide”. Biotechnol. Bioengng 1998; 59: 273–276
   PubMedGoogle Scholar
• Lee H., Park G. T. “Conjugation of trypsin by temperature-sensitive polymers containing a carbohydrate moiety: thermal modulation of enzyme activity”. Biotechnol. Prog 1998; 14: 508–516
   PubMed Web of Science ®Google Scholar
• Matsukata M., Aoki T., Sanui K., Ogata K., Kikuchi A., Sakurai Y., Okana T. “Effect of molecular structure of poly(N-isopropylacrylamide)-trypsin conjugates on their solution and enzymatic properties”. Bioconjugate Chem 1998; 7: 96–101
   Web of Science ®Google Scholar
• Monji N., Hoffman A. S. “A novel immunoassay system and bioseparation process based on thermal phase separating polymers”. Appl. Biochem. Biotechnol 1987; 14: 107–120
   PubMed Web of Science ®Google Scholar
• Mosbach K. “Immobilized enzymes”. Methods Enzymol. Academic Press, New York 1976; vol. 44
   Google Scholar
• Murphy A., ófágáin C. “Chemically stabilized trypsin used in dipeptide synthesis”. Biotechnol. Bioengng 1998; 58: 366–373
   PubMed Web of Science ®Google Scholar
• Nagayama H., Maeda Y, Shimasaki C., Kitano H. “Catalytic properties of enzymes modified with temperature-responsive polymer chains”. Macromol. Chem. Phys 1995; 196: 611–620
   Web of Science ®Google Scholar
• O'Neil S. P., Wykes J. R., Dunnill P., Lilly M. D. “An ultrafiltration reactor system using a soluble immobilized enzyme”. Biotechnol. Bioengng 1971; 13: 319–322
   Web of Science ®Google Scholar
• Park T. G., Hoffman A. S. “Synthesis and characterization of a soluble, temperature-sensitive polymer-conjugated enzyme”. J. Biomater. Sci Polymer Edn 1993; 4: 493–504
   PubMed Web of Science ®Google Scholar
• Senstad C., Mattiasson B. “Affinity precipitation using chitosan as ligand carrier”. Biotechnol. Bioengng 1989; 33: 216–220
   PubMed Web of Science ®Google Scholar
• Schild H. G. “Poly(N-isopropylacrylamide): experiment, theory and application”. Prog. Polym. Sci 1992; 17: 163–249
   Web of Science ®Google Scholar
• Schild H. G., Tirrell D. A. “Microcalorimetric detection of lower critical solution temperature in aqueous polymer solutions”. J Phys. Chem 1990; 94: 4352–4356
   Web of Science ®Google Scholar
• Simon L. M., Lászlo K., Vértesi A., Bagi K., Szajáni B. “Stability of hydrolytic enzymes in water-organic solvent systems”. J Mol. Catal. B: Enz 1998; 4: 41–45
   Google Scholar
• von Spechet B. U., Brendel W. “Preparation and properties of trypsin and chymotrypsin coupled covalently to poly(N-vinylpyrrolidone)”. Biochim. Biophys. Acta 1977; 484: 109–114
   PubMedGoogle Scholar
• Stayton P. S., Shimoboji T., Long C, Chilkoti A., Chen G., Harris J. M., Hoffman A. S. “Control of protein-ligand recognition using a stimuli-responsive polymer”. Nature 1995; 378: 472–474
   PubMed Web of Science ®Google Scholar
• Tanaka X, Nishio I., Sun S. T., Nishio S. U. “Collapse of gels in an electric field”. Science 1982; 218: 467–469
   PubMed Web of Science ®Google Scholar
• Wykes J. R., Dunnill P., Lilly M. D. “Immobilisation of α-amylase by attachment to soluble support materials”. Biochim. Biophys. Acta 1971; 250: 522–529
   PubMed Web of Science ®Google Scholar