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The use of graft copolymers as enzyme supports (1979)

Beddows, C. G. ; Mirauer, R. A. ; Guthrie, J. T. ; [et al.]

Springer

Polymer bulletin 1 (1979), S. 749-753

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ISSN: 1436-2449

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics

Notes: Summary A new type of polymer support for immobilizing enzymes, a copolymer grafted onto nylon was investigated. Polyacrylamide was used and successfully coupled to β-galactosidase (from yeast and bacteria) using two different methods to give activities of the order of 5 units/g of polymer for the yeast enzyme, and 156 units/g for the E.coli enzyme. Lactose did not affect the yield. The azide method gave better results than the glutaraldehyde method. β-galactosidase coupled enzyme was fairly stable but not as good as the free enzyme. Papain was also coupled to the polyacrylamide grafted nylon using both methods; the glutaraldehyde gave better results with 1.5mg of enzyme being coupled for each gram of polymer.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00256275

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Immobilization of β-galactosidase and other enzymes onto p-amino-carbanilated cellulose derivatives (1980)

Beddows, C. G. ; Mirauer, R. A. ; Guthrie, J. T.

New York, NY [u.a.] : Wiley-Blackwell

Biotechnology and Bioengineering 22 (1980), S. 311-321

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ISSN: 0006-3592

Keywords: Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: β-Galactosidase and other enzymes were immobilized on p-amino-carbanilated derivatives of cellulose and methylol cellulose using the diazo method and through glutaraldehyde. The optimum conditions for coupling cellulose tri-(p-amino-carbanilate) (CTAC) to β-galactosidase were established. The diazo coupling method with CTAC gave greater activity than with glutaraldehyde when coupled to β-galactosidase (Escherichia coli). The stability of the CTAC-β-galactosidase system was examined. The disubstituted p-amino-carbanilate derivative (CDAC) gave a lower activity, whereas the methylol analog (MCTAC) gave slightly greater activity. The CTAC was also used to immobilize glucose oxidase, trypsin, pepsin, and papain.

Additional Material: 5 Ill.