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1.
J Colloid Interface Sci ; 293(1): 248-51, 2006 Jan 01.
Artículo en Inglés | MEDLINE | ID: mdl-16112680

RESUMEN

Low-pressure argon adsorption has been used to study the energetic distribution of microporous activated carbons differing by their burn-off. The collected isotherms were analyzed using the derivative isotherm summation method. Some oscillations on the experimental curves for very low partial pressures were detected. The results are analyzed and discussed according to the literature and could be attributed to local overheating caused by spontaneous mass transfer of argon through constrictions between former pores and the new opening pore or deadend pores. We used the dynamic character of the experimental method and mainly the discrepancy of the quasi-equilibrium state to deduce key parameters related to the porosity topology.

2.
J Colloid Interface Sci ; 285(1): 56-60, 2005 May 01.
Artículo en Inglés | MEDLINE | ID: mdl-15797395

RESUMEN

The adsorption of water vapor on a microporous activated carbon derived from the carbonization of coconut shell has been studied. Preadsorption of naphthalene was used as a tool to determine the location and the influence of the primary adsorbing centers within the porous structure of active carbon. The adsorption was studied in the pressure range p/p0=0-0.95 in a static water vapor system, allowing the investigation of both kinetic and equilibrium experimental data. Modeling of the isotherms using the modified equation of Do and Do was applied to determine the effect of preadsorption on the mechanism of adsorption.

3.
Gene ; 123(1): 115-9, 1993 Jan 15.
Artículo en Inglés | MEDLINE | ID: mdl-8422994

RESUMEN

An aminopeptidase P (PepP)-encoding gene has been cloned from Streptomyces lividans 66 by screening for overexpression of activity using the chromogenic substrate Gly-Pro-beta-naphthylamide as a liquid overlayer on colonies growing on agar medium. The pepP gene was localised by deletion mapping, and the nucleotide sequence was determined. The deduced amino acid sequence was found to display significant similarity to Escherichia coli PepP. The partially purified S. lividans enzyme had a 50-kDa subunit and was present as a homodimer. Direct Edman degradation of the purified protein confirmed that pepP encoded the observed intracellular PepP.


Asunto(s)
Aminopeptidasas/genética , Genes Bacterianos , Streptomyces/genética , Secuencia de Aminoácidos , Aminopeptidasas/metabolismo , Secuencia de Bases , Clonación Molecular , ADN Bacteriano , Biblioteca Genómica , Datos de Secuencia Molecular , Mapeo Restrictivo , Homología de Secuencia de Aminoácido , Streptomyces/enzimología
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