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  • 1
    Electronic Resource
    Electronic Resource
    Investigation of the immobilisation of bovine serum albumin, trypsin, acid phosphatase and alkaline phosphatase to poly(hydroxyethyl acrylate)-co-cellulose and poly(hydroxyethyl acrylate)-co-pectin (1984)
    Springer
    Polymer bulletin 11 (1984), S. 1-6 
    Details
    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 Poly(hydroxyethyl methacrylate)-co-pectins (107% graft), activated with p-benzoquinone, immobilised 122 mg of bovine serum albumin (BSA) per g of copolymer and 22.4 mg of trypsin per g of copolymer. This latter figure was replicated when p-toluene sulphonyl chloride was used for activating the copolymer. In a separate exercise p-benzoquinone was used to couple diaminohexane to the copolymer. This modified product immobilsed 396 mg of trypsin/g when glutaraldehyde was used in coupling. A 25% grafted, poly(hydroxyethyl methacrylate)-co-cellulose immobilised 39.5 mg of BSA per g of copolymer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401706
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  • 2
    Electronic Resource
    Electronic Resource
    Cellulose Derivatives Membranes as Supports for Immobilisation of Enzymes (1998)
    Springer
    Cellulose 5 (1998), S. 299-308 
    Details
    ISSN: 1572-882X
    Keywords: glucose oxidase ; alcohol oxidase ; catalase ; cellulose derivatives ; enzyme immobilisation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Cellulosic derivatives (cellulose acetate, cellulose propionate and cellulose acetate-butyrate) as membranes, were prepared in different ways. These were then characterised by differential scanning calorimetry (DSC), scanning electron microscopy (SEM) and contact angle evaluation. Subsequently, catalase (H2O2:H2O2 oxireductase; EC 1.11.1.6), alcohol oxidase (Alcohol:oxygen oxireductase; EC 1.1.3.13) and glucose oxidase (β-D- Glucose:oxygen 1-oxireductase; EC 1.1.3.4) were covalently linked to these membranes. The catalytic activity and stability of these enzymes, when immobilised, were examined. The results obtained showed that the immobilisation efficiency and the stability of the coupled enzymes could be correlated with the studied properties of the supports. The cellulose acetate membrane which was prepared by evaporation gave the more active conjugate support-enzyme. Membranes prepared by the immersion technique were more crystalline and therefore less suitable for enzyme immobilisation. The highly hydrophobic membranes, obtained from the propionate and the butyrate esters of cellulose reduced the activities but gave better storage stability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1009255126274
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of cellulose derivatives — Relevance to sensor development (1995)
    Springer
    Cellulose 2 (1995), S. 243-263 
    Details
    ISSN: 1572-882X
    Keywords: cellulose acetate ; cellulose acetate butyrate ; ethyl cellulose ; characterization ; biosensor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract With the aim of developing a urea biosensor, several cellulose derivatives were used to coat an all-solid-state potentiometric electrode for ammonium ion determination. In this work the physical and chemical characterization of the cellulose derivatives, as well as the changes that the activation and immobilization procedures induced in the polymers, were studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00811816
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  • 4
    Electronic Resource
    Electronic Resource
    The immobilisation of bovine serum albumin, acid phosphatase, glucose oxidase and phenyl propylamine to maleic anhydride block copolymers (1985)
    Springer
    Polymer bulletin 14 (1985), S. 199-206 
    Details
    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 Maleic anhydride-based block copolymers have been prepared by various routes. These copolymers provide the basis for enzyme immobilisation without the need for secondary coupling agents. It is felt that problems arising from enzyme-support interactions are much reduced relative to systems using poly(acrylic acid)-branch supports. There are problems in stability in that these supports cannot be used above a pH of 7.4. At low pH values, gel formation arises. Such gel formation enhances the immobilisation efficiency considerably but generates media which are difficult to process. Ease of coupling was a feature of non-aqueous systems, suggesting that products obtained in this way should be of use in affinity separations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00254938
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  • 5
    Electronic Resource
    Electronic Resource
    Microcapsules prepared from starch derivatives (1997)
    Springer
    Journal of materials science 8 (1997), S. 321-323 
    Details
    ISSN: 1573-4838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract In this work, vinyl groups were introduced on soluble starch by reaction with 2-vinyl-4,4-dimethyl-2-oxazolin-5-one. The polysaccharides obtained were characterized by 1H-NMR and DSC. The 1H-NMR spectra showed high degrees of substitution and the DSC thermograms suggest a low crystallinity in the modified starch. The modified starch was used to obtain microcapsules prepared through interfacial crosslinking with DPGDA (dipropyleneglycol diacrylate) by a water-in-oil emulsion polymerization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018568513662
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  • 6
    Electronic Resource
    Electronic Resource
    The immobilizaton of enzymes, bovine serum albumin, and phenylpropylamine to poly(acrylic acid)-polyethylene-based copolymers (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 1371-1387 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A poly(acrylic acid)-polyethylene graft copolymer was prepared and used initially to couple to acid phosphatase, using soluble carbodiimides. Yields which were quite good were obtained with CMC but not with EDAC. The copolymers was used to couple trypsin using EEDQ. Several organic solvents were investigated for the preparation of the “activated” poly(acrylic acid) intermediate. Using the activated system, high concentrations of trypsin were bound but the relative activities were not very high. The yield was good with bovine serum albumin (BSA). When the method was used for invertase, acid phosphatase, and alkaline phosphatase, the yields were poor and the copolymer was shown to absorb protein by an ion-exchange mechanism. However, the activated system gave a good yield of coupling to phenylpropylamine. A polyethylene-coacrylic-acid polymer containing 13% of acrylic acid (by weight) was then converted to the acid chloride by refluxing with thionyl chloride. The chlorinated copolymer which contained 0.7% chlorine and a thionyl-chloride-treated polyethylene control which contained no chlorine were investigated in immobilization studies. Such coupling involved bovine serum albumin (BSA), alkaline phosphatase, trypsin, β-galactosidase, and invertase. Bovine serum albumin coupled well to the support, but none of the enzymes gave high levels of enzymes activity. Phenylpropylamine coupled well and all of the acid chloride groups were involved. Tyrosine reacted with 63% of the available acid chloride groups.
    Additional Material: 7 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260240610
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  • 7
    Electronic Resource
    Electronic Resource
    Immobilization of BSA, enzymes and cells of Bacillus stearothermophilus onto cellulose, polygalacturonic acid and starch based graft copolymers containing maleic anhydride (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 51-57 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Poly(maleic anhydride styrene) graft copolymers of cellulose, pectin polygalacturonic acid salt, calcium polygalacturonate, and starch were prepared and used to immobilize proteins. The cellulose grafts coupled quite appreciable quantities of acid phosphatase, glucose oxidase, and trypsin. However, the general retention of activity was somewhat disappointing. Further investigation with acid phosphatase showed that the amount of enzyme immobilized increased as the amount of anhydride in the graft copolymer increased but no such relationship existed for the enzymic activity. The cellulose graft copolymers were hydrolyzed and it appeared that the carboxyl group aided adsorption of the enzyme. Attempts to couple acid phosphatase using CMC through the free carboxyl groups, created by hydrolysis, gave only a small increase in the extent of protein coupling. However, the unhydrolyzed system gave a useful degree of immobilization of cells of Bacillus stearothermophilus, as did a poly(maleic anhydride/styrene)-cocellulose system. Attempts to improve the activity by using grafts based on other polysaccharide supports met with mixed success. Pectin products were soluble. Polygalacturonic acid products were partially soluble and extremely high levels of enzymic activity were obtained. This was probably due in part to the hydrophilic nature of the system, which also encouraged absorption of the enzyme. Attempts were made to reduce the solubility by using the calcium pectinate salt. Immobilization of acid phosphatase and trypsin resulted in inceased protein coupling but relatively poor activities were attained. A starch based system gave similar results. Calcium polygalacturonate was used to prepare an insoluble graft copolymeric system containing acrylonitrile-comaleic anhydride. The resulting gels gave excellent coupling with acid phosphatase which had a very good retention of activity.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280108
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilization of α-chymotrypsin onto hydrolyzed poly(ethylene)-g-co-hydroxyethyl methacrylate (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 41 (1990), S. 1629-1639 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: α-Chymotrypsin has been immobilized onto partially hydrolyzed poly(ethylene)-g-co-hydroxyethyl methacrylate (120% graft), using 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide-p-toluene-sulphonate (CMC) as the activating agent. The influence of the enzyme concentration, the carbodiimide concentration, and the coupling medium on the immobilization reaction was studied. A system with 160 mg of coupled enzyme per gram copolymer, providing 126 mg of active enzyme per gram of copolymer was obtained. The KM, Vmax, and the optimum temperature profile and optimum pH value for the free and immobilized α-chymotrypsin were determined.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1990.070410722
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  • 9
    Electronic Resource
    Electronic Resource
    Behaviour of catalase immobilised on poly(acrylonitrile)-g.co-hydroxyethyl methacrylate when used in a continuous system (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Polymer International 38 (1995), S. 269-275 
    Details
    ISSN: 0959-8103
    Keywords: graft copolymer ; catalase ; immobilisation ; continuous system ; acrylonitrile ; hydroxyethyl methacrylate ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Several poly(acrylonitrile)-g.co-hydroxyethyl methacrylate graft copolymers were prepared using gamma irradiation (60Co). The influences of the monomer concentration and the time of irradiation on the level of grafting were studied. Some of the graft copolymers obtained were characterised and used for the covalent immobilisation of catalase using two different methods of activation of the support.The enzyme/support systems obtained were characterised and the best selected to be used in a first approach for the study of the deterioration of a hydrogen peroxide solution in a continuous system.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pi.1995.210380309
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  • 10
    Electronic Resource
    Electronic Resource
    The immobilization of enzymes onto hydrolyzed polyethylene-g-co-2-HEMA (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 35 (1988), S. 135-144 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A study of the immobilization of trypsin and other enzymes onto hydrolyzed poly(2-hydroxyethyl methacrylate)-g-co-polyethylene using hydroxyl and carboxyl activating agents has been undertaken. Some emphasis was placed on the immobilized trypsin system which involved examination of the variation of (i) the extent of hydrolysis of the graft copolymer, (ii) the concentration of activating agent, and (iii) the temperature of coupling. With the trypsin system, an increase in carbodi-imide concentration gave an increase in the amount of protein immobilized but a marked decrease in the retention of enzymic activity. Comparison of the behavior of the free with the immobilized enzyme showed that satisfactory yields were obtained and the immobilized system has an extended pH profile and good stability and thus would have broad applicability. The kinetic factors were examined further, and the role of the graft copolymer chains in the immobilized system is discussed.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1988.070350112
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