Stability performance of Cynara cardunculus L. acid protease in aqueous-organic biphasic systems

M. T. Barros; M. G. V. Carvalho; F. A. P. Garcia; E. M. V. Pires

doi:10.1007/BF01023355

Stability performance of Cynara cardunculus L. acid protease in aqueous-organic biphasic systems

M. T. Barros, M. G. V. Carvalho, F. A. P. Garcia, E. M. V. Pires^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

Abstract

Stability performance of the acid protease of Cynara cardunculus L. in biphasic systems containing ethyl acetate, n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containing n-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases of n-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.

Original language	English
Pages (from-to)	179-184
Number of pages	6
Journal	Biotechnology Letters
Volume	14
Issue number	3
DOIs	https://doi.org/10.1007/BF01023355
Publication status	Published - Mar 1992
Externally published	Yes

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title = "Stability performance of Cynara cardunculus L. acid protease in aqueous-organic biphasic systems",

abstract = "Stability performance of the acid protease of Cynara cardunculus L. in biphasic systems containing ethyl acetate, n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containing n-hexane. In this system 100\% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases of n-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.",

author = "Barros, \{M. T.\} and Carvalho, \{M. G. V.\} and Garcia, \{F. A. P.\} and Pires, \{E. M. V.\}",

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T1 - Stability performance of Cynara cardunculus L. acid protease in aqueous-organic biphasic systems

AU - Barros, M. T.

AU - Carvalho, M. G. V.

AU - Garcia, F. A. P.

AU - Pires, E. M. V.

PY - 1992/3

Y1 - 1992/3

N2 - Stability performance of the acid protease of Cynara cardunculus L. in biphasic systems containing ethyl acetate, n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containing n-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases of n-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.

AB - Stability performance of the acid protease of Cynara cardunculus L. in biphasic systems containing ethyl acetate, n-hexane or isooctane was investigated and compared with that of pepsin. Activity retention was higher in the system containing n-hexane. In this system 100% retention was observed up to 144 hours. Pre-saturation of phases was found to increase enzyme stability in the cases of n-hexane and isooctane and to be an absolute requirement in the case of ethyl acetate. The results obtained suggest also that, when dealing with pre-saturated phases, log P cannot be used straightforwardly to predict enzyme stability in biphasic systems.

UR - https://www.scopus.com/pages/publications/0026606763

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VL - 14

SP - 179

EP - 184

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 3

ER -

Stability performance of Cynara cardunculus L. acid protease in aqueous-organic biphasic systems

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