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  • 1
    Electronic Resource
    Electronic Resource
    Activities of Enzymes of Sugar Metabolism in Gamma-Irradiated Potato Tubers (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The sucrose content of potato tubers was increased by gamma-irradiation. The activities of enzymes responsible for sugar metabolism in irradiated potato tubers were measured during storage after irradiation. The activities of phosphorylase, sucrose synthase and sucrose phosphate synthase were significantly enhanced by irradiation and remained at a high level while sucrose was accumulated in irradiated tubers. The activities of phosphoglucomutase and phosphoglucose isomerase were little influenced by irradiation. The activity of UDP-glucose pyrophosphorylase was enhanced slightly by irradiation and decreased to a level lower than unirradiated tubers depending upon irradiation dose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb09201.x
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  • 2
    Electronic Resource
    Electronic Resource
    Accumulation of Sucrose in Gamma-Irradiated Sweet Potato Roots (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 47 (1982), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of storage conditions on the sucrose content of gamma-irradiated sweet potato roots was studied. The sucrose content was influenced mainly by the temperature and oxygen content of the atmosphere. The degree of sucrose accumulation decreased, as the oxygen content of the atmosphere was reduced, while it increased with increase of temperature. The best conditions for the accumulation of sucrose were an irradiation dose of 1 kGy and a storage temperature of 30°C. The sucrose content of the roots which were irradiated and stored under the above conditions exceeded 12% on a fresh weight basis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb12933.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes by radiocopolymerization of monomers (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 17 (1975), S. 599-605 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260170411
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Immobilization of microbial cells containing NAD-kinase (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1019-1030 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Microbial cells having NAD-kinase activity, Brevibacterium ammoniagenes, were immobilized by the radiation-copolymerization method under low temperature with the activity recovery of more than 80%. Compared to the native microbial cells the immobilized cells were more stable against heat and pH change. The immobilized cells were subjected to the 5 hr reaction repeatedly 20 times without any activity loss.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210607
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  • 5
    Electronic Resource
    Electronic Resource
    Production of NADP by immobilized cells with NAD kinase (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 857-869 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: By the radiation-copolymerization method with polyethylene glycoldimethacrylate (PGD) as a main polymerizable reagent, microbial cells of Brevibacterium ammoniagenes were immobilized with high specific activity of NAD kinase and high mechanical strength. The reagents used for the immobilization such as PGD, polyvinyl alcohol (PVA), and N,N′-methylenebisacrylamide (Bis) did not inversely affect the enzyme activity. Freezing and irradiation treatment of the cell-reagent solution did not inactivate the enzyme either, but longer freezing time or a lower irradiation dose (less than 400 krad) resulted in the unsatisfactory mechanical strength of the immobilized cells. Almost all of NAD and ATP consumed were converted into NADP within three hours reaction time. The drum reactor was found to be ideal for the reaction of immobilized cells, since it gave little mechanical stress to the immobilized cells for the effective mixing of the cells and the substrates. The immobilized cells were subjected to three hours reaction repeatedly for 30 times without any activity loss.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260240409
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  • 6
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes by radiopolymerization of acrylamidePart 1 in a series of studies on the preparation of immobilized enzymes by radiopolymerization. An outline of the work described here was presented at the annual meeting of the Agricultural Chemical Society of Japan, April 1973, Tokyo. (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 16 (1974), S. 609-621 
    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 new and simple method for immobilization of enzymes by the aerobic radio-polymerization of acrylamide was developed. Irradiation treatment of acrylamide in the frozen state produces a spongy immobilized enzyme membrane without the addition of carriers. Aerobic polymerization yields of acrylamide in the frozen state were increased by the addition of starch and also by lyophilization.Glucose oxidase (activity recovery was 12.3-33.7%), invertase (69.2%), D-amono acid oxidase (25.0-70.5%), aminoacylase (39.2-43.7%), mold α-amylase (18.0%), malt β-amylase (4.1%), glucoamylase (6.5%), alkaline protease (5.3%), and neutral protease (10.5%) were immobilized by this method. Invertase entrapped by this method had a wider optium pH range and was active at higher temperatures.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260160505
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  • 7
    Electronic Resource
    Electronic Resource
    Immobilization of the exo-maltohexaohydrolase by the irradiation method (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1095-1107 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Exomaltohexaohydrolase (E.C.3.2.1.98) was immobilized by radiocopolymerization of some synthetic monomers which were mixed in various combinations. Irradiation was carried out while the mixture of monomers and enzymes was frozen in petroleum ether-dry-ice bath. Recovery of the immobilized enzyme was 44-75%.The optimum pH of the enzyme slightly shifted to the acidic side. The pH stability was improved remarkably by immobilization. The enzyme was stable retaining more than 90% of its original activity in the range pH 4-11. The optimum reaction temperature of the enzyme increased about 2°C. Heat stability was also improved by immobilization, and that the enzyme retained about 40% of its original activity after treatment at 75°C for 15 min. The immobilized enzyme was stable to the repeated use of 20 cycles. The Km value of the enzyme for short-chain amylose was almost the same as that of native enzyme. When soluble starch was used as the substrate, the Km, value of the enzyme was three times as large as that of native enzyme. Effects of various metal ions and inhibitors on the immobilized enzyme were also studied compared to the native enzyme.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250417
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