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  • Biochemistry and Biotechnology  (2)
  • Z 1 region  (1)
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  • 1
    ISSN: 1573-2754
    Keywords: stress structure ; singularity ; Z 1 region ; stress triaxialityRσ ; CTOD ; shear lip ; interpolative method ; degree parameter of the plane strain state
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Mathematics , Physics
    Notes: Abstract Based on [1], the stress structures of the smooth region and shear lip of the specimens have been investigated in the paper. The characteristics of the stress structure in the smooth region have been found that the variable z can separated out; the stresses in the midsection can be obtained by the plane strain FEM results or HRR structure modified by the stress triaxiality. The effects of load level and thickness on the stress structure can be reflected by the distribution of CTOD along the thickness direction. The obtained expressions of the stresses are very simple and visualized. The analyses of the stress structure in the shear lip show that the stresses can be obtained by different methods of interpolation to a certain precise degree. A new degree parameter of the plane strain state has been put forward and studied. The parameter can reflect relatively well the variation of the kind and thickness of the specimen as well as the load level. The fracture parameter has also been investigated to be sure that it can be obtained by modified CTOD with the stress triaxiality.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 46 (1995), S. 172-174 
    ISSN: 0006-3592
    Keywords: reversed micelles ; extraction ; trypsin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: By using trypsin as the model protein and AOT as the model surfactant, the effect of a variety of solvents on protein transfer and activity recovery during the liquid-liquid reversed micellar extraction was investigated. It was found that several solvents, including isooctane, octane, heptane, and kerosene, had a similar effect on the recovery of trypsin activity after a full cycle of forward and backward extraction, and could all be used as the solvents for AOT-reversed micelles in trypsin extraction. Two other solvents (hexane and cyclohexane), however, were not so efficient. © 1995 John Wiley & Sons, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 48 (1995), S. 745-748 
    ISSN: 0006-3592
    Keywords: Aliquat 336 ; reversed micelles ; purification ; α-amylase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The purification of industrial α-amylase by liquid-liquid extraction with Aliquat 336 reversed micellar solution as the extractant was studied. Seven kinds of Aliquat 336 reversed micellar solution, formed by using seven kinds of straight chain alkyl alcohols as cosolvent, have been utilized to extract industrial a-amylase. It was found that these seven kinds of reversed micellar solution can all achieve a high protein transfer efficiency in the forward extraction process. After a full forward and backward extraction cycle, however, only the reversed micelles with n-butanol as the cosolvent was found to be able to maintain the activity of α-amylase in the stripping solution. By using the reversed micelles of Aliquat 336/isooctane/1% (v/v) n-butanol to perform a full extraction cycle, it was found that 85% of the total activity of α-amylase in the industrial a-amylase could be recovered at the end of an extraction cycle and the specific activity of α-amylase could be concentrated about 1.5-fold; meanwhile, most of the neutral protease in the industrial a-amylase could be removed. The separation factor of α-amylase to neutral protease at the end of an extraction cycle can reach about 10. © 1995 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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