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pro vyhledávání: '"E. Battistel"'
Akademický článek
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Autor:
E. Battistel, G. Rialdi
Publikováno v:
Journal of Thermal Analysis. 47:17-25
The thermal stability of papain in free solution or immobilized on CPC-silica has been investigated by DSC. At neutralpH, in both conditions, the protein undergoes a thermal transition which corresponds to the sum of two transitions associated with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::50d6b0ad857567615e506af75f01f5c5
https://doi.org/10.1007/bf01982682
https://doi.org/10.1007/bf01982682
Autor:
E. Battistel, G. Rialdi
Publikováno v:
Journal of Thermal Analysis. 45:631-637
Recent progress in thermodynamic aspects of proteins, free or immobilized on solid support, are described. In agreement with results observed with Ribonuclease A [9], DSC analysis on α-chymotrypsin confirms a decoupling of melting domains with the i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2733c438fe088ef8459f57b5c75ef51
https://doi.org/10.1007/bf02548877
https://doi.org/10.1007/bf02548877
Publikováno v:
Applied Microbiology and Biotechnology. 43:508-513
A screening of microorganisms producing glutaryl-7 ADCA acylase, an enzyme able to hydrolyse glutaric acid selectively from glutaryl-3-deacetoxy-7-aminocephalosporanic acid (glutaryl-7 ADCA), has been carried out in soil samples. Five microorganisms
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdaea2ba9b98349747967734bb3b7b1a
https://doi.org/10.1007/bf00218457
https://doi.org/10.1007/bf00218457
Autor:
E. Battistel, D. Bianchi
Publikováno v:
The Journal of Physical Chemistry. 98:5368-5375
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::352bf1d7ad803c286433c4ba98947fe2
https://doi.org/10.1021/j100071a030
https://doi.org/10.1021/j100071a030
Akademický článek
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Publikováno v:
Journal of Thermal Analysis. 38:159-167
Recent progress in thermodynamic aspects of protein function in unusual environments are described. Systems considered include enzymes incorporated in reverse micelles, immobilized onto solid support or suspended in low-water solvents.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f19ec5da4b69a43e4a9c57e032081a0
https://doi.org/10.1007/bf02109116
https://doi.org/10.1007/bf02109116
Publikováno v:
Thermochimica Acta. 172:21-30
Isothermal batch calorimetry can give useful information on the biological activity of enzymes immobilized on solid supports. As a model system, the enthalpy change and the apparent equilibrium constant of the cytidine-3'-monophosphate binding to sol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ea17dc4fb90fda3573740158bf71eb8
https://doi.org/10.1016/0040-6031(90)80556-e
https://doi.org/10.1016/0040-6031(90)80556-e
Publikováno v:
All Days.
The filter cake removal is still an important concern both for producers and injectors. Mainly in long horizontal completion sections, the cleanup of the filter cake does not always occur spontaneously because sometimes the drawdown in the production
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d530fa49840b96d8ca3a22608dbe284
https://doi.org/10.2118/94702-ms
https://doi.org/10.2118/94702-ms
Lipase fromCandida rugosa was stabilized against thermal inactivation in the presence of polyvinylalcohols (PVA) of different molecular weights. The apparent rate constant of the lipase inactivation, kd, at 49°C is 0.049/min and 0.022/min in the abs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ee6fbca35c758bb70a697e643414c9a
http://hdl.handle.net/11386/3017567
http://hdl.handle.net/11386/3017567
