Abstract
The literature abounds with procedures to immobilize enzymes which generally fit into one of six main categories. The earliest methods developed were enzyme adsorption and cross-linking. Adsorption-cross-linking, the combination of these methods, results in a more utilitarian catalyst. The most widely used method is covalent bonding of the enzyme to a support material; but entrapment and microencapsulation are valuable techniques for immobilization of enzymes.
The properties of immobilized enzymes are affected by the support material. In essence, the physical properties are those of the support material. Inorganic supports result in rigid catalysts with moderate enzyme loading. Very high enzyme loading can be achieved with organic supports which are easily molded into desired shapes. The support used for immobilization of enzymes also affects the chemical properties of the catalyst. The optimum pH is often different for an immobilized enzyme than for the soluble enzyme and changes in substrate specificity have also been observed.
Immobilized enzymes find applications both in industrial processing and analytical testing. In addition, immobilized enzymes have been used for analysis of the structure-function relationships of enzymes. Although showing considerable promise, therapeutic applications generally remain in the research stage.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
A. Wiseman, in: Handbook of Enzyme Biotechnology (A. Wiseman, ed.), pp. 111–124, Wiley, New York (1975).
M. Keyes, Encyclopedia of Chemical Technology, Vol. 9, 148–172, Wiley, New York (1980).
T. Everse, C. L. Ginsburg, and N. O. Kaplan, Methods Biochem. Anal. 25, 135–201 (1977).
J. S. Holcenberg and J. Roberts, ed., Enzymes as Drugs, pp. 1–353, Wiley, New York (1981).
P. J. Lisi, T. van Es, A. Abuchowski, N. C. Palczuk, and F. F. Davis,J. Appl Biochem. 4, 19–33 (1982).
C. H. W. Hirs, ed., Methods in Enzymology, Vol. 11, pp. 481–640, Academic Press, New York (1967).
C. H. W. Hirs and S. N. Timasheff, ed., Mewthods in Enzymology, Vol. 25, pp. 339–651, Academic Press, New York (1972).
M. A. Mitz and L. J. Summaria, Nature {London) 169, 576–577 (1961).
P. W. Carr and L. D. Bowers, Immobilized Enzymes in Analytical and Clinical Chemistry, Wiley, New York (1980).
L. B. Wingard, E. Katchalski-Katzir and L. Goldstein, eds., Applied Biochemical Bioengineering, Vol. 1, Academic Press, New York (1976).
I. Chibata, Immobilized Enzymes, Wiley, New York (1978).
T. K. Ghose, A. Fiechter, and N. Blakebrough, eds., Advanced Biochemical Engineering, Vol. 10, Springer-Verlag, New York (1978).
R. A. Messing, ed., Immobilized Enmzymes for Industrial Reactors, Academic Press, New York (1975).
K. Mosbach, ed., Methods in Enzymology, Vol. 44, Academic Press, New York (1976).
L. B. Wingard, Jr., E. Katchalski-Katzir, and L. Goldstein, eds. Applied Biochemical Bioengineering, Vol. 3, Academic Press, New York (1981).
A. C. Olson and C. L. Cooney, eds., Immobilized Enzymes Food Microbiology Processes, (Proceedings of Symposium), Plenum Press, New York (1974).
M. Salmona, C. Saronio, and S. Garottini, eds., Insolubilized Enzymes, Raven Press, New York (1974).
T. M. S. Chang, ed., Biomedical Applied Immobilized Enzymes Proteins, Vol. 1, Plenum Press, New York (1977).
R. A. Messing, in: Advanced Biochemical Engineering (T. K. Ghose, A. Fiechter, and N. Blakebrough, eds.), Vol. 10, pp. 51–73, Springer-Verlag, New York (1978).
G. P. Royer, G. M. Green, and B. K. Sinha, in: Polymer Grafts in Biochemistry (H. F. Hixson, Jr. and E. P. Goldberg, eds.), pp. 289–307, Marcel Dekker, New York (1976).
O. Zaborsky, in: Biomedical Applications of Immobilized Enzymes and Proteins (T. M. S. Chang, ed.), p. 37, Plenum Press, New York (1977).
R. A. Messing, Biotechnol. Bioeng. 16, 897–908 (1974).
P. Grunwald, W. Gunsser, F. R. Heiker, and W. Roy, Anal. Biochem. 100, 54–57 (1979).
G. A. Kovalenki, N. B. Shitova, and U. D. Sokolowski, Biotechnol. Bioeng. 23, 1721–1734 (1981).
R. Uy and F. Wold, in: Advanced Experimental Medical Biology (M. Friedman, ed.), Vol. 86A, pp. 169–186, Plenum Press, New York (1977).
F. M. Richards and J. R. Knowles,J. Mol. Biol. 37, 231–233 (1968).
P. Monsan, G. Puzo, and H. Mozargui, Biochimie 57, 1281–1292 (1975).
R. Haynes and K. A. Walsh, Biochem. Biophys. Res. Commun. 36, 235–242 (1969).
R. Haynes and K. A. Walsh, U.S. Patent No. 3,796,634 (1974).
M. H. Keyes, U.S. Patent No. 3,933,589 (1976).
M. H. Keyes, U.S. Patent No. 4,008,126 (1977).
M. H. Keyes, U.S. Patent No. 4,204,040 (1980).
R. A. Messing, U.S. Patent No. 3,804,719 (1974).
G. Brown, E. Selegny, S. Avrameas, and D. Thomas, Biochim. Biophys. Acta 185, 260–262 (1969).
J. Porath, in: Methods in Enzymology (W. B. Jacoby and M. Wilchek, eds.), Vol. 34, pp. 13–30, Academic Press, New York (1974).
J. Porath and R. Axen, in: Methods in Enzymology (K. Mosbnach, ed.), Vol. 44, pp. 19–42, Academic Press, New York (1976).
M. D. Lilly, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 46–53, Academic Press, New York (1976).
I. Chibata, Immobilized Enzymes, pp. 15–46, Wiley, New York (1978).
R. Axen and S. Ernback, Eur. J. Biochem. 1971, 21 351–360.
R. Axen, J. Porath, and S. Ernback, Nature(London) 214, 1302–1304 (1967).
R. Axen and P. Vretblad, Acta Chem. Scand. 25, 2711–2716 (1971).
R. L. Schnaar, T. F. Sparks, and S. Roseman, Anal. Biochem. 79, 513–525 (1977).
M. Wilchek, T. Oka, and Y. J. Trooper, Proc. Natl. Acad. Sci. U.S.A. 72, 1055–1058 (1975).
K. Kohn and M. Wilchek, Biochem. Biophys. Res. Commun. 84, 7–14 (1978).
J. Kohn and M. Wilchek, Anal. Biochem. 115, 375–382 (1981).
J. Kohn and M. Wilchek, Enzyme Microb. Technol. 4, 161–164 (1982).
H. Rosemeyer, E. Körnig, and F. Seela, Eur. J. Biochem. 122, 375–380 (1982).
L. R. Benkova, M. Mrackova, and K. Baber, Collect. Czech. Chem. Commun. 45, 160–167 (1980).
M. Iwaki and M. Nozaki,J. Biochem.(Tokyo) 91, 1549–1553 (1982).
M. Wilchek, in: Enzyme Engineering (E. K. Pye and H. H. Weetall, eds.), Vol. 3, pp. 283–289, Plenum Press, New York (1978).
J. F. Kennedy and J. A. Barnes, Int. J. Biol. Macromol. 2, 289–296 (1980).
T. Oka and Y. J. Trooper, Proc. Natl. Acad. Sci. U.S.A. 71, 1630–1636 (1974).
M. Wilchek and T. Miron, in: Methods in Enzymology (W. B. Jakoby and M. Wilchek, eds.), Vol. 34, pp. 72–76, Academic Press, New York (1974).
O. Hannibal-Friedrich, M. Chun, and M. Sernetz, Biotechnol. Bioeng. 22, 157–175 (1980).
I. Matsumoto, H. Kitagaki, Y. Akai, Y. Ito, and N. Seno, Anal. Biochem. 116, 103–110 (1981).
I. Matsumoto, Y. Mizuno, and H. Seno, J. Biochem. (Tokyo) 85, 1091–1098 (1979).
L. Sundberg and J. Porath, J. Chromatogr. 90, 97–98 (1974).
K. Nilsson, O. Norrlow, and K. Mosbach, Acta Chem. Scand., Ser, B 35, 19–27 (1981).
K. Nilsson and K. Mosbach, Biochem. Biophys. Res. Commun. 102, 449–457 (1981).
L. Bulow and K. Mosbach, Biochem. Biophys. Res. Commun. 107, 456–464 (1982).
T. H. Finlay, V. Troll, M. Levey, A. J. Johnson, and L. T. Hodgins, Anal. Biochem. 87, 77–90 (1978).
G. Kay and M. D. Lilly, Biochim. Biophys. Acta 198, 276–285 (1970).
C. Smith and H. M. Lenhoff, Anal. Biochem. 61, 302–305 (1974).
P. Cuatrecasas and I. Parikh, Biochemistry 11, 2291–2298 (1972).
R. G. Frost, J. F. Monthony, S. C. Engelhorn, and C. J. Siebert, Biochim. Biophys. Acta 670, 163–169 (1981).
S. A. Berker, H. C. Tun, D. H. Doss, C. J. Gray, and J. F. Kennedy, Carbohydr. Res. 17, 471–474 (1971).
J. F. Kennedy and A. Zamir, Carbohydr. Res. 29, 497–501 (1973).
C. J. Grey and T. H. Yeo, Carbohydr. Res. 27, 2325–238 (1973).
J. Porath, T. Laas, and J. C. Janson,J. Chromatogr. 103, 49–62 (1975).
J. Brandt, L. Andersson, and J. Porath, Biochim. Biophys. Acta 386, 196–202 (1967).
M. Singh, A. R. Ray, P. Vasudevan, P. Verma, and S. K. Guha, Biomater. Med. Dev. Artif. Organs 7, 495–512 (1979).
F. B. Weakley and C. L. Mehltretter, Biotechnol Bioeng. 15, 1189–1192 (1973).
S. A. Barker and J. F. Kennedy, in: Handbook of Enzyme Biotechnology (A. Wiseman, ed.), pp. 203–209, Wiley, New York (1975).
L. A. Cohen, in: Methods in Enzymology (W. B. Jakoby and M. Wilchek, eds.), Vol. 34, pp. 103–108, Academic Press, New York (1974).
K. Brocklehurst, J. Carlsson, M. P. J. Kiersten, and E. M. Crook, Biochem. J. 133, 573–584 (1973).
J. S. Lin and J. F. Foster, Anal. Biochem. 63, 485–490 (1975)
J. Carlsson, R. Axen, and T. Unge, Eur. J. Biochem. 59, 567–572 (1975).
J. Carlsson, R. Axen, K. Brocklehurst, and E. M. Crook, Eur. J. Biochem. 44, 189–194 (1974).
R. Axen, O. Vretblad, and J. Porath, Acta Chem. Scand. 25, 1129–1132 (1971).
P. Vretblad and R. Axen, Acta Chem. Scand. 27, 2769–2780 (1973).
L. Goldstein, J. Chromatogr. 215, 31–43 (1981).
H. H. Weetall, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 134–148, Academic Press, New York (1976).
A. Wiseman, in: Topics in Enzyme Fermentation Biotechnology (A. Wiseman, ed), Vol. 2, pp. 49–57, Halsted Press, New York (1978).
H. H. Weetall, Nature (London) 223, 959–960 (1969).
H. H. Weetall, in: Advanced Experimental Medical Biology (R. B. Dunlap, ed.), Vol. 42, pp. 191–212, Plenum Press, New York (1974).
W. F. Line, H. Wong, and H. H. Weetall, Biochim. Biophys. Acta 242, 194–202 (1971).
H.H. Weetall and A. M. Filbert, in: Methods in Enzymology (W. B. Jakoby and M. Wilchek, eds.), Vol. 34, pp. 295–297, Academic Press, New York (1974).
M. V. Wondolowski and T. H. Woychik, Biotechnol. Bioeng. 16, 1633–1654 (1974).
B. E. Dale and D. H. White, Biotechnol. Bioeng. 21, 1639–1648 (1979).
K. Parkin and H. O. Hultin, Biotechnol. Bioeng. 21, 939–953 (1979).
V. Ramesh and C. Singh,J. Appl. Biochem. 4, 81–85 (1982).
B. Danielsson, B. Mattiason, R. Karlsson, and F. Winqvist, Biotechnol. Bioeng. 21, 1749–1766 (1979).
C. C. Hon and P. J. Reilly, Biotechnol. Bioeng. 21, 505–511 (1979).
O. V. Lomako, I. I. Menyailova, C. A. Nakhapetyan, Y. Nikitin, and A. V. Kiselev, Enzyme Microb. Technol. 4, 89–92 (1982).
C. D. Bowers and P. B. Johnson, Anal. Biochem. 116, 111–115 (1981).
G. P. Royer, F. A. Liberatore, and G. M. Green, Biochem. Biophys. Res. Commun. 64, 478–484 (1975).
L. D. Bowers and P. W. Carr, Anal. Chem. 48, 549–558 (1976).
J. M. Cabrai, J. M. Nováis, and J. P. Cardoso, Biotechnol. Bioeng. 23, 2083–2092 (1981).
R. D. Mason and H. H. Weetall, Biotechnol Bioeng. 14, 637–645 (1972).
B. Weiss, M. Hui, and A. Lajtha, Biochem. Med. 18, 330–343 (1977).
T. Mori, F. Sato, T. Tosa, and I. Chibata, Enzymologia 43, 217–226 (1972).
S. E. Brolin, A. Agren, B. Ekman, and S. Joholm, Anal. Biochem. 78, 577–581 (1977).
A. Szewczuk, A. Ziomek, M. Mordarski, M. Siewinski, and J. Wieczorek, Biotechnol. Bioeng. 21, 1543–1552 (1979).
K. F. O’Driscoll, in: Methods in Enzoymology (K. Mosbach, ed.), Vol. 44, pp. 169–175, Academic Press, New York (1976).
K. F. O’Driscoll, M. Izu, and R. Korus, Biotechnol. Bioeng. 14, 847–850 (1972).
S. Fukui, A. Tanaka, T. Iida, and E. Hasegawa, FEBS Lett. 66, 179–182 (1976).
I. Kaetsu, K. Minoru, and Y. Yoshida, Biotechnol. Bioeng. 21, 847–861 (1979).
J. Dobo, Acta Chim. Acad. Sci. Hung. 63, 453–456 (1970).
K. Kawashima and K. Umeda, Biotechnol. Bioeng. 16, 609–621 (1979).
K. Kawashima and K. Umeda, Agric. Biol. Chem. 40, 1151–1157 (1979).
I. Kaetsu, M. Kumakura, and M. Yoshida, Biotechnol. Bioeng. 21, 847–861 (1979).
H. Maeda, H. Suzuki, and A. Yamauchi, Biotechnol Bioeng. 15, 607–610 (1973).
H. Maeda, H. Suzuki, and A. Yamauchi, Biotechnol. Bioeng. 15, 827–829 (1973).
T. Yagi, Appl. Biochem. 1, 448–454 (1979).
V. Jancsik, Z. Belezani, and T. Keleti, J. Mol. Catal 54 297–306 (1982).
T. Tosa, T. Sato, K. Mori, I. Yamamoto, Y. Takata, Y. Nishida, and I. Chibata, Biotechnol. Bioeng. 21, 1697–1707 (1979).
Y. Y. Linko, L. Pohtola, R. Viskari, and M. Linko, FEBS Lett. 62, 77–80 (1976).
E. K. Bauman, L. H. Goodson, G. G. Guilbault, and D. N. Kramer, Anal. Chem. 37, 1378–1381 (1965).
A. Pollak, H. Blumenfeld, M. Wax, R. Bughn, and G. M. Whiteside,J. Am. Chem. Soc. 102, 6326–6336 (1980).
L. D’Angiuro, P. Cremonesi, G. Mazzola, B. Fochev, and G. Vecchio, Biotechnol. Bioeng. 22, 2251–2272 (1980).
L. D’Angiuro, G. Mazzola, G. Vecchio, B. Fochev, and P. Cremonesi, J. Appl. Biochem. 2, 208–217 (1980).
T. M. S. Chang, Nature (London) 229, 117–118 (1971).
T. Mori, T. Tosa, and I. Chibata, Biochim. Biophys. Acta 321, 653–661 (1973).
R. D. Aisina and G. B. Nakdarni, Biotechnol. Bioeng. 23, 431–436 (1981).
I. Chibata, Immobilized Enzymes, pp. 57–59, Wiley, New York (1978).
D. Dinelli, W. Marconi, and F. Morisi, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 227–231, Academic Press, New York (1978).
G. Gregoriadis, N. Engl. J. Med. 295, 706–710 (1976).
G. Gregoriadis, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 218–227, Academic Press, New York (1976).
M. B. Fiddler, C. D. S. Hudson, and R. J. Desnick, Biochim. J. 168, 191–195 (1977).
M. H. Keyes, U.S. Patent No. 3,839,175 (1974).
I. Karube and S. Suzuki, Biochem. Biophys. Res. Commun. 47, 51–54 (1972).
W. R. Vieth and K. Venkatasubramanian, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 248–250, Academic Press, New York (1976).
A. M. Klibanov, Anal. Biochem. 93, 1–25 (1979).
H. H. Weetall, Biochim. Biophys. Acta 212, 1–7 (1970).
W. H. Pitcher, Jr., in: Advanced Biochemical Engineering (T. K. Ghose, A. Fiechter, and N. Blakebrough, eds.), Vol. 10, pp. 1–26, Springer-Verlag, New York (1978).
D. L. Regan, P. Dunnill, and M. D. Lilly, Biotechnol. Bioeng. 16, 333–343 (1974).
P. W. Carr and L. D. Bowers, Immobilized Enzymes in Analytical and Clinical Chemistry, pp. 249–251, Wiley, New York (1980).
D. Gabel, I. Z. Steinberg, and E. Katchalski, Biochemistry 10, 4661–4669 (1971).
I. Chibata, Immobilized Enzymes, pp. 168–178, Wiley, New York (1978).
K. A. Hughes, Wall Street Journal (Three Star), East Ed., November 9, 1982, p. 31.
P. Brodelius, in: Industrial Applications of Immobilized Biocatalysts in Advanced Biochemical Engineering (T. K. Ghose, A. Fiechter, and N. Blakebrough, ed.), Vol. 10, pp. 75–109, Springer-Verlag, New York (1978).
P. W. Carr and L. D. Bowers, Immobilized Enzymes in Analytical and Clinical Chemistry, pp. 197–299, Wiley, New York (1980).
B. Danielsson, I. Lundstrom, K. Mosbach, and L. Stiblert, Anal. Lett. 12, 1189–1199 (1979).
K. Mosbach, U.S. Patent No. 4,021,307 (1977).
L. D. Bowers and P. W. Carr, Thermochim. Acta 10, 129–142 (1974).
J. C. Weaver, C. L. Cooney, S. P. Fulton, P. Schuler, and S. R. Tannenbaum, Biochim. Biophys. Acta 452, 258–291 (1976).
L. C. Clark, Jr., U.S. Patent No. 3,539,455 (1970).
S. J. Updike and G. P. Hicks, Nature (London) 214, 986–988 (1967).
B. Mattiasson and B. Danielsson, Carbohydr. Res. 102, 273–282 (1982).
B. Danielsson, K. Gaold, B. Mattiasson, and K. Mosbach, Anal. Lett. 9,987–1001 (1976).
W. J. Blaedel and R. A. Jenkins, Anal. Chem. 48, 1240–1247 (1976).
G. G. Guilbault and E. Hrabankova, Anal. Chem. 42, 1779–1783 (1970).
M. Nanjo and G. G. Guilbault, Anal. Chim. Acta 75, 167–180 (1975).
G. J. Papariello, A. K. Mukherji, and C. M. Shearer, Anal. Chem. 45, 790–792 (1973).
G. P. Hicks and J. J. Updike, Anal. Chem. 38, 726–730 (1966).
M. H. Keyes and R. C. Barabino, in: Enzyme Engineering (E. K. Pye and H. H. Weetall, eds.), Vol. 3, pp. 51–56, Plenum Press, New York (1976).
B. Watson and M. H. Keyes, Anal. Lett. 9, 713–725 (1976).
B. Watson, D. N. Stifel, and F. E. Semersky, Anal. Chim. Acta 106, 233–242 (1979).
B. Volesky and C. Emond, Biotechnol. Bioeng. 21, 1251–1276 (1979).
P. R. Johnson and L. D. Bowers, Anal. Chem. 54, 2247–2250 (1982).
D. J. Inman and W. E. Hornby, Biochem. J. 137, 25–32 (1974).
D. R. Senn, P. W. Carr, and L. N. Klatt, Anal. Chem. 48, 954–963 (1976).
G. Johansson, K. Edstrom, and L. Ogren, Anal. Chim. Acta 85, 55–60 (1976).
R. C. Barabino, D. N. Gray, and M. H. Keyes, Clin. Chem. (Winston-Salem, N.C.), 24, 1393–1398 (1978).
L. Ogren and G. Johansson, Anal. Chim. Acta 96, 1–11 (1978).
D. N. Gray, M. H. Keyes, and B. Watson, Anal. Chem. 49, 1067A–1072A (1977).
D. N. Gray, and M. H. Keyes, CHEMTECH 7, 642–648 (1977).
I. Chan, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 491–503, Academic Press, New York (1976).
G. F. Bickerstaff, Int. J. Biochem. 11, 201–206 (1980).
S. McCraken and E. Meighen, Can. J. Biochem. 57, 834–842 (1979).
J. S. Holcenberg, Ann. Rev. Biochem. 57, 795–812 (1982).
G. Gregoriadis, in: Methods in Enzymology (K. Mosbach, ed.), Vol. 44, pp. 698–709, Academic Press, New York (1976).
G. Gregoriadis, N. Engl. J. Med. 295, 765–770 (1976).
G. Gregoriadis and E. D. Neerunjun, Eur. J. Biochem. 7, 179–185 (1974).
R. L. Juliano and D. Stamp, Biochem. Biophys. Res. Commun. 63, 651–658 (1975).
P. Gosh, P. K. Das, and B. K. Bachhawat, Arch. Biochem. Biophys. 213, 266–270 (1982).
L. D. S. Hudson, M. B. Fiddler, and R. J. Desnick, J. Pharmacol. Exp. Ther. 208, 507–514 (1979).
G. A. Grabowski and R. J. Desnick, in: Enzymes as Drugs (J. C. Holcenberg and J. Roberts, eds.), pp. 167–208, Wiley-Interscience, New York (1981).
I. V. Berezin and S. D. Varfolomeev, Appl. Biochem. Bioeng. 2, 259–290 (1979).
E. C. Hatchikian and P. Monsan, Biochim. Biophys. Res. Commun. 92,1091–1096 (1980).
D. A. Lappi, F. E. Stolzenbach, N. O. Kaplan, and M. D. Kamen, Biochem. Biophys. Res. Commun. 69, 878–884 (1976).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1985 Plenum Press, New York
About this chapter
Cite this chapter
Keyes, M.H., Saraswathi, S. (1985). Immobilized Enzymes. In: Gebelein, C.G., Carraher, C.E. (eds) Bioactive Polymeric Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0405-1_11
Download citation
DOI: https://doi.org/10.1007/978-1-4757-0405-1_11
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-0407-5
Online ISBN: 978-1-4757-0405-1
eBook Packages: Springer Book Archive