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  • 1
    Electronic Resource
    Electronic Resource
    Application of Sucrose Synthase from Rice Grains for the Synthesis of Carbohydrates (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 750 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb19975.x
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  • 2
    Electronic Resource
    Electronic Resource
    Engineering Aspects of Enzyme (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 613 (1990), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1990.tb18157.x
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  • 3
    Electronic Resource
    Electronic Resource
    TECHNICAL ASPECTS OF EXTRACTIVE ENZYME PURIFICATION (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 369 (1981), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1981.tb14201.x
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  • 4
    Electronic Resource
    Electronic Resource
    The application of Nα-formyl amino acid esters in the enzyme-catalyzed peptide synthesis (1988)
    Springer
    Monatshefte für Chemie 119 (1988), S. 1323-1331 
    Details
    ISSN: 1434-4475
    Keywords: Enzyme catalyzed peptide synthesis ; Formyl protecting group ; Optical purity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Abstract Die Synthese Nα-Formyl-geschützter Aminosäureester und deren Anwendung in der kinetisch kontrollierten α-Chymotrypsin-, Trypsin- und CarboxypeptidaseY-katalysierten Peptidsynthese wird beschrieben. Man erhält hierbei optisch einheitliche Produkte, was anhand der Synthese von H-Tyr-Ala-OH gezeigt wurde. Reaktionsausbeuten bei Verwendung verschiedener Ester werden diskutiert. Im Verhältnis zu gängigen α-Aminoschutzgruppen der chemischen Peptidsynthese weisen Nα-Formyl-geschützte Derivate in wäßrig-alkoholischen Medien verbesserte Löslichkeiten auf.
    Notes: Abstract The synthesis of Nα-formyl protected amino acid esters and their use in kinetically controlled α-chymotrypsin-, trypsin- and carboxypeptidaseY-catalyzed peptide synthesis is described. Using the synthesis of H-Tyr-Ala-OH as example it is demonstrated that optically uniform products are obtained. Reaction yields are discussed with regard to the ester component employed. In comparison to commonly used α-amino protecting groups in chemical peptide synthesis, Nα-formyl amino acid derivatives show improved solubilities in aqueous-alcoholic media.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00808313
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  • 5
    Electronic Resource
    Electronic Resource
    Large scale production of d-lactate dehydrogenase for the stereospecific reduction of pyruvate and phenylpyruvate (1983)
    Springer
    Applied microbiology and biotechnology 18 (1983), S. 75-85 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary To initiate studies of the stereospecific reduction of pyruvate and phenylpyruvate to the corresponding d-2-hydroxyacids a limited screening was carried out for microorganisms possessing a high NADH-dependet d-lactate dehydrogenase activity. Lactobacillus confusus was found to produce the desired dehydrogenase, which showed also relatively high activity towards phenylpyruvate, so this strain was selected for large scale production of the enzyme. A procedure for large scale purification of the enzyme starting with 24 kg wet cells is described including liquid-liquid extraction, ultrafiltration and chromatography on DEAE-cellulose, yielding a catalyst with specific activities of 216 U×mg−1 for pyruvate reduction and 15 U×mg−1 for phenyl-pyruvate reduction. A further tenfold purification can be achieved by affinity chromatography on Blue-Sepharose C-6B. Parameters which are important for industrial application of the enzyme were determined: substrate specifity, pH and temperature optimum, temperature stability, stability at different pH-values, and the storage stability of the enzyme in crude extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00500828
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  • 6
    Electronic Resource
    Electronic Resource
    Production of hydantoinase fromPseudomonas fluorescens strain DSM 84 (1986)
    Springer
    Applied microbiology and biotechnology 25 (1986), S. 91-96 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Pseudomonas fluorescens strain DSM 84 was selected as a good hydantoinase (dihydropyrimidinase E.C. 3.5.2.2.) producer from a screening involving 60 collection strains. Optimization of the culture and growth conditions were performed in order to increase the enzyme production. A mineral medium supplemented with 10 g/l of yeast extract having an initial pH of 7.1±0.1 but containing no additional carbon source or inducer was devised. The strain DSM 84 was found to produce the maximal level of hydantoinase in the defined mineral medium within 15 h of incubation at 27°C. When using 5-isopropylhydantoin as substrate, N-carbamyl-valine was detected as the end product of the crude hydantoinase. Conditions leading to the isolation and conservation of a crude hydantoinase as well as its temperature and pH stability are described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00938930
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  • 7
    Electronic Resource
    Electronic Resource
    Isolation of l-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of l-phenylalanine (1987)
    Springer
    Applied microbiology and biotechnology 26 (1987), S. 409-416 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary l-Phenylalanine dehydrogenase [l-phenylalanine: NAD+-oxidoreductase (deaminating)] of Rhodococcus sp. strain M4 was studied emphasizing its application for the production of l-phenylalanine. A high enzyme level (30,000 U·l-1, 25–30 U·mg-1 in the crude extract) could be reached during aerob degradation of l-phenylalanine (10 g·l-1) under optimized growth coditions. A partial purification of the intracellular enzyme by liquid-liquid extraction, and DEAE-cellulose led to a specific activity of more than 1300 U·mg-1. The continuous production of l-phenylalanine in an enzyme-membrane-reactor for 350h resulted in a space-time yield of 456 g·l-1·d-1 with a mean substrate conversion of 95%. Consumption of phenylalanine dehydrogenase was 1,500 U·kg Phe-1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00253523
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  • 8
    Electronic Resource
    Electronic Resource
    Screening for a novel enzyme hydrolysing l-carnitine amide (1994)
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 599-605 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract. In an extended screening using d,l-carnitine amide as carbon or nitrogen source about 1300 strains were obtained by enrichment culture. Of these, 65 strains possessed carnitine amidase activities. A single strain was identified as containing an enzyme able to hydrolyse only l-carnitine amide and yield carnitine of high enantiomeric purity (≥97) when incubated with the racemic substrate. During the initial optimisation of the culture conditions the volume activity could be improved 6.7-fold whereas the specific activity increased 3.6-fold. The enzyme is inducible by l-carnitine amide and carnitine and to a lesser degree also by γ-butyrobetaine and dehydrocarnitine. As judged by the fatty acids and quinone composition the strain belongs into the α-subgroup of purple bacteria but has not yet been classified by the German Culture Collection into a known genus of bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050035
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  • 9
    Electronic Resource
    Electronic Resource
    Catalytic properties and substrate specificity of 3-hexulose phosphate synthase fromMethylomonas M15 (1991)
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 604-607 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary 3-Hexulose phosphate synthase was purified in 94% yield from Methylomonas M15. The enzyme did not form a Schiff-base intermediate with d-ribulose 5-phosphate that could be reduced by NaBH4. However, the enzyme required Mg2+ or Mn2+ ions for activity and was inactivated in the presence of EDTA. The latter is a property of class II aldolases. The enzyme accepted a wide range of other aldehydes in addition to its natural substrate formaldehyde, while d-ribulose 5-phosphate could not be replaced. This makes it an attractive tool for the synthesis of higher sugar phosphates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00167907
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  • 10
    Electronic Resource
    Electronic Resource
    l-leucine dehydrogenase fromBacillus cereus (1985)
    Springer
    Applied microbiology and biotechnology 22 (1985), S. 306-317 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An improved method for the production ofl-leucine dehydrogenase is described employing a mutant with a constitutive enzyme and a fed-batch cultivation technique yielding high cell concentrations. Purification ofl-leucine dehydrogenase to homogeneity was carried out starting with 30 kgBacillus cereus cells by heat treatment at 63°C, followed by two liquid-liquid extraction steps and three conventional column chromatographies. Crystals have been obtained from the 95-fold purified enzyme. The molecular weight of the native enzyme was determined by sedimentation equilibrium and gel filtration studies to be 310 000 containing eight identical subunits with a molecular weight of 39 000. The sedimentation coefficient was estimated to 11.65 S. Branched-chain amino acids likel-leucine,l-valine orl-isoleucine are deaminated by the NAD-dependent enzyme. In the reverse reaction a variety of 2-ketoacids, especially 2-ketoisocaproate, 2-ketoisovalerate and 2-keto-3-methyl-valerate, were reductive aminated to the correspondingl-amino acids in the presence of 0.9 M ammonia. The amino acid composition for the subunit ofl-leucine dehydrogenase is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00582413
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