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  • FLUID MECHANICS AND HEAT TRANSFER  (342)
  • Biochemistry and Biotechnology  (270)
  • 2020-2024
  • 1985-1989  (605)
  • 1955-1959  (7)
Collection
Keywords
Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    An evaluation of the performance of ten commercial luminometers (1989)
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 3 (1989), S. 131-145 
    Details
    ISSN: 0884-3996
    Keywords: Luminometer ; evaluation ; rapid microbiology ; ATP assay ; firefly luciferase ; photometer ; radiometer ; comparison ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: An assessment has been carried out of the relative performance of ten instruments for quantification of adenosine triphosphate (ATP) by the firefly luciferase assay. The instruments evaluated were Amersham Amerlite Analyser, Dynatech Tube Luminometer, Dynatech Multiplate Luminometer, Dynatech Camera Luminometer, Hamilton Lumicon, LKB 1250 Luminometer, LKB 1251 Luminometer, Lumac Biocounter M2010A, Turner 20 TD Luminometer and a prototype version of the CLEAR Speed Tech 2000. An 800-fold difference in sensitivity was found between the most sensitive (Lumac, Turner) and the least sensitive (Dynatech Tube) of the conventional instruments. The Dynatech Camera Luminometer which worked on a completely different principle to the other instruments was about 5000 times less sensitive than the best of the photomultiplier tube instruments. The relative sensitivity of the instruments was maintained regardless of whether solutions of ATP in water or trichloroacetic acid extracts of bacteria were analysed. An analysis of 960 ATP bioluminescence assays showed that data obtained from such measurements are normally distributed.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bio.1170030307
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  • 2
    Electronic Resource
    Electronic Resource
    Lipase-catalyzed ester exchange reactions in organic media with controlled humidity (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 30 (1987), S. 258-266 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilized lipase activity is studied in organic solvent systems of controlled water content under the influence of a variety of reaction parameters, such as temperature, relative humidity, substrate concentrations, and type of fatty acid used. Control of the amount of water in the reaction system was found to be a valuable tool for the orientation of the reaction process and for the determination of the final reaction products. The properties of the immobilized lipase were studied using the interesterification of triolein and palmitic acid as the model system.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260300216
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  • 3
    Electronic Resource
    Electronic Resource
    Optimization of steam explosion as a method for increasing susceptibility of sugarcane bagasse to enzymatic saccharification (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 733-741 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The technique of autohydrolysis steam explosion was examined as a means for pretreatment of sugarcane bagasse. Treatment conditions were optimized so that following enzymatic hydrolysis, pretreated bagasse would give 65.1 g sugars/100 g starting bagasse. Released sugars comprised 38.9 g glucose, 0.6 g cellobiose, 22.1 g xylose, and 3.5 g arabinose, and were equivalent to 83% of the anhydroglucan and 84% of the anhydroxylan content of untreated bagasse. Optimum conditions were treatment for 30 S with saturated steam at 220°C with a water-to-solids ratio of 2 and the addition of 1 g H2SO4/100 g dry bagasse. Bagasse treated in this manner was not inhibitory to fermentation by Saccharomyces uvarum except at low inoculum levels when fermentation time was extended by up to 24 h. Pretreated saccharified bagasse was inhibitory to Pachysolen tannophilus and this was attributed to the formation of acetate from the hydrolysis of acetyl groups present in hemicellulose. The major advantage of the pretreatment is the achievement of high total sugar yield with moderate enzyme requirement and only minor losses due to sugar decomposition.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290610
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  • 4
    Electronic Resource
    Electronic Resource
    Phospholipids in chromatin: Incorporation of [32P]O42- in different subcellular fractions of hepatocytes (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 4 (1986), S. 283-288 
    Details
    ISSN: 0263-6484
    Keywords: Chromatin ; phospholipid synthesis ; rat hepatocytes ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Nuclear, chromatin and microsomal fractions were isolated from hepatocytes prepared from rats injected with [32P] O42- and killed subsequently at times between 1 and 48 h. Specific activities of the total phospholipids (PL) were determined for each subcellular fraction. The major points noted were (a) the initial specific activity of the chromatin PL was half that of both nuclear and microsomal PL at 1 h; (b) the first peak of labelling occurred at 6 h in both nuclear and microsomal PL, but was 3 h later (9h) in the chromatin PL; and (c) a second peak of labelling occurred in the chromatin and microsomal PL, but not in those of the nuclei.On fractionation of the PL, the major and most metabolically active components were phosphatidylcholine + phosphatidylethanolamine, whilst sphingomyelin accounted for only about 8 per cent of the total PL. The chromatin and microsomal fractions were somewhat similar in their labelling patterns though with a delayed peaking of activity in the chromatin. This is indicative of a synthesis and transport of PL from the microsomes to the chromatin.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290040409
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  • 5
    Electronic Resource
    Electronic Resource
    The relationship between tissue preparation and function; methods for the study of control of aldosterone secretion: A review (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 3 (1985), S. 235-253 
    Details
    ISSN: 0263-6484
    Keywords: Aldosterone ; adrenal cortex ; zona glomerulosa ; in vitro incubation ; steroid hormones ; secretion ; tissue preparation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The study of the control of aldosterone synthesis and secretion by the rat adrenal gland has over the past thirty years involved the application of many different in vivo and in vitro techniques. In this review the relationship between the data that each of these methods has produced is compared. There are striking differences in overall steroid production rates, and in the qualitative nature of the steroid profile which the various methods produce. In particular, aldosterone is secreted at higher rates in vivo, and when whole tissue preparations are used in vitro, than in incubations of isolated glomerulosa cells. In addition, while corticosterone is a major product of glomerulosa tissue in vitro, the available evidence suggests that it is not a major glomerulosa product in vivo.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290030402
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  • 6
    Electronic Resource
    Electronic Resource
    Immobilization of a soluble chemically thermostabilized enzyme (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 572-578 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cellobiase was coupled to a dialdehyde dextran by reductive alkylation in the presence of sodium cyanoborohydride. The resulting conjugate, obtained without loss of enzymic activity, presents properties of thermoresistance largely superior to those of native enzyme: the rate of inactivation is reduced compared to that of native enzyme and its optimal temperature of activity is 70-75°C instead of 65°C. Finally the conjugate presents increased longevity when subjected to experiments of operational stability; its hydrolytic activity is maintained at 60°C in a 10% (w/v) cellobiose solution for more than 100 h whereas the native enzyme is inactivated after 45 h. The cellobiase-dextran conjugate was immobilized by covalent coupling on aminated silica by reductive alkylation in the presence of NaBH3CN. The characteristics of thermoresistance of this stabilized and immobilized conjugate were studied and compared to those of a preparation of native cellobiase immobilized on a silica support activated with glutaraldehyde. Analysis of the thermoresistance of these two cellobiase preparations clearly shows that immobilization has maintained and even enhanced their properties. In particular, the operational stability, measured at 68°C on 10% (w/v) cellobiose shows an increased longevity of the stabilized and immobilized enzyme for 120 h compared to 60 h for the native immobilized enzyme. Two successive incubations of these cellobiase derivatives show that it is possible to obtain 2.5 times more glucose with the stabilized-immobilized enzyme than with the immobilized preparation. The procedure described above enables us to prepare a thermostabilized immobilized cellobiase.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270505
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  • 7
    Electronic Resource
    Electronic Resource
    Separation of ethanol from ethanol - water mixture by reverse osmosis (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 27 (1985), S. 1081-1084 
    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: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260270725
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation and purification of protease from human placenta by foam fractionation (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 29 (1987), S. 934-940 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effect of operating parameters like pH, protein concentration, column geometry, and gas flow rate on the separation efficiency of proteolytic enzymes from crude human placental homogenate has been studied in a batch foam column. Purification has been found to be optimum at pH 8.0, close to the isoelectric pH, at which the surface adsorption of the protein on the foam bubbles is maximum. Both purification and recovery varied significantly with total protein concentration. Stable bubble formation was hindered at lower protein concentrations, while extraneous proteins rather than the protease were preferentially adsorbed at higher protein concentrations, decreasing the purification efficiency. Column diameter and column height should be optimized for any specific feed protein concentration and gas flow rate. However, the enrichment ratio was found to decrease with the increase in flow rate. The results indicate that foam fractionation is an effective separation process for recovering valuable biochemicals from biological materials.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260290804
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  • 9
    Electronic Resource
    Electronic Resource
    Biohydrogenation of unsaturated fatty acids by a mixed culture of rumen microorganisms (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1268-1276 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The biohydrogenation of C-18 unsaturated fatty acids was examined in a mixed culture of microorganisms prepared by inoculating a proper growth medium with a sample of rumen fluid. Some major factors influencing the hydrogenation capacity have been investigated. The age of the mixed culture, the type of inoculum used, the concentration of substrates as well as the presence of sterile rumen fluid in the growth medium were found to be important factors determining biohydrogenation behavior. It could be shown that the mixed microbial culture, which had been grown for about 24 h on a medium similar to that of Bryant and Robinson, contained sterile rumen fluid (10% v/v), and had been inoculated with a sample of the whole untreated rumen content, had the best biohydrogenation capacity. The culture was able to carry out the complete conversion of linoleic and linolenic acid to stearic acid.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260280820
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  • 10
    Electronic Resource
    Electronic Resource
    Large-scale production of monoclonal antibodies in suspension culture (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 993-1000 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Monoclonal antibodies are being manufactured for clinical trials in suspension culture at the 1300-L scale. Suspension culture offers some advantages relative to high-density mammalian cell culture methods; in particular, the ability to closely monitor the behavior of cells in a homogeneous environment. Computer control and on-line mass spectrography of exit gases provide instantaneous information about the culture metabolic activity. Air sparging and agitation by marine impeller provide aeration sufficient to maintain a constant dissolved oxygen tension at cell concentrations up to 5.0 × 106 cells/mL without causing apparent cell damage.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320807
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