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  • 1995-1999  (3)
  • Biochemistry and Biotechnology  (3)
  • coenzyme regeneration  (1)
  • fed-batch process  (1)
  • endoglucanase
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Years
Year
Keywords
  • 1
    ISSN: 0006-3592
    Keywords: glucose-fructose oxidoreductase ; Zymomonas mobilis ; free enzyme ; continuous production ; stability ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: For the continuous, enzymatic synthesis of sorbitol and gluconic acid by cell-free glucose-fructose oxidoreductase (GFOR) from Zymomonas mobilis, the principal determinants of productivity have been identified. Most important, the rapid inactivation of the soluble enzyme during substrate conversion can be avoided almost completely when weak bases such as tris(hydroxymethyl)aminomethan or imidazol are used for the titration of the produced gluconic acid and when 5-10 mM dithiothreitol are added to prevent thiol oxidations. With regard to a long-term operational stability of the enzyme for continuous syntheses, thermal deactivation becomes significant at reaction temperatures above 30°C. Without any additional purification being required, the crude cell extract of Z. mobilis can be employed in a continuous ultrafiltration membrane reactor over a time period of more than 250 h without significant decrease in substrate conversion or enzyme activity. The use of soluble GFOR thus appears to be an interesting alternative to employing permeabilized cells of Zymomonas for the production of sorbitol and gluconic acid and may be superior with regard to reactor productivities, at comparable operational stabilities. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 53: 623-629, 1997.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 52 (1996), S. 387-396 
    ISSN: 0006-3592
    Keywords: xylitol ; NADH regeneration ; charged membrane ; continuous production ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: We have developed a new process for the production of xylitol from D-xylose by enzyme technology. An NADH-dependent xylose reductase (XR) from Candida tenuis catalyzes the reduction of xylose, which is coupled to enzymatic oxidations of D-glucose or D-xylose by glucose dehydrogenase from Bacillus cereus to make achievable an up to 10,000-fold regeneration of NADH per cycle of discontinuous conversion. Using a simple kinetic model as a tool for process optimization, suitable conditions with regard to performance and stability of the multi-component reaction system were established, and 300 g/L of substrate could be converted in yields above 96% in one single batch reaction. Due to selective and over 98% complete retention of the native coenzyme by negatively charged nanofiltration membranes used in a continuously operated enzyme reactor, a specific productivity of 80 g xylitol per liter, day, and kilounit of XR was maintained over the 150-h reaction time with only a single dosage of NADH. © 1996 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0006-3592
    Keywords: coenzyme regeneration ; formate dehydrogenase ; fed-batch process ; xylitol production ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The NAD-dependent, formate dehydrogenase-catalyzed oxidation of formate anion into CO2 is known as the method for the regeneration of NADH in reductive enzymatic syntheses. Inhibition by formate and inactivation by alkaline pH-shift that occurs when oxidation of formate is carried out at pH ≈ 7.0 may, however, hamper the efficient application of this NADH recycling reaction. Here, we have devised a fed-batch process using pH-controlled feeding of formic acid that can overcome enzyme inhibition and inactivation. The reaction pH is thus kept constant by addition of acid, and formate dehydrogenase is supplied continuously with substrate as required, but the concentration of formate is maintained at a constant, non- or weakly inhibitory level throughout the enzymatic conversion, thus enabling a particular NADH-dependent dehydrogenase to operate stably and at high reaction rates. For xylitol production from xylose using yeast xylose reductase (Ki,Formate 182 mM), a fed-batch conversion of 0.5M xylose yielded productivities of 2.8 g (L h)-1 that are three-fold improved when contrasted to a conventional batch reaction that employed equal initial concentrations of xylose and formate. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 60: 277-282, 1998.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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