High hydrostatic pressure inactivation kinetics of the plant proteases ficin and papain

Katsaros, GI; Katapodis, P; Taoukis, PS

dc.contributor.author	Katsaros, GI	en
dc.contributor.author	Katapodis, P	en
dc.contributor.author	Taoukis, PS	en
dc.date.accessioned	2014-03-01T01:30:50Z
dc.date.available	2014-03-01T01:30:50Z
dc.date.issued	2009	en
dc.identifier.issn	0260-8774	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/19646
dc.subject	Enzyme kinetics	en
dc.subject	Ficin	en
dc.subject	High pressure	en
dc.subject	Papain	en
dc.subject	Thermal inactivation	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.classification	Food Science & Technology	en
dc.subject.other	Activation energy	en
dc.subject.other	Catalysts	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	Enzymes	en
dc.subject.other	Food processing	en
dc.subject.other	Hydrostatic pressure	en
dc.subject.other	Ketones	en
dc.subject.other	Proteins	en
dc.subject.other	Rate constants	en
dc.subject.other	Activation volumes	en
dc.subject.other	Ambient pressures	en
dc.subject.other	Antagonistic effects	en
dc.subject.other	Different effects	en
dc.subject.other	Effect of pressures	en
dc.subject.other	Effect of temperatures	en
dc.subject.other	Ficin	en
dc.subject.other	High hydrostatic pressures	en
dc.subject.other	High pressure	en
dc.subject.other	High pressures	en
dc.subject.other	High thermals	en
dc.subject.other	Higher temperatures	en
dc.subject.other	Inactivation kinetics	en
dc.subject.other	Inactivation rates	en
dc.subject.other	Increasing effects	en
dc.subject.other	Papain	en
dc.subject.other	Parameter equations	en
dc.subject.other	Plant proteases	en
dc.subject.other	Pressure conditions	en
dc.subject.other	Pressure increases	en
dc.subject.other	Pressure stabilities	en
dc.subject.other	Process conditions	en
dc.subject.other	Process pressures	en
dc.subject.other	Process temperatures	en
dc.subject.other	Temperature sensitivities	en
dc.subject.other	Thermal inactivation	en
dc.subject.other	Thermal processes	en
dc.subject.other	High pressure liquid chromatography	en
dc.title	High hydrostatic pressure inactivation kinetics of the plant proteases ficin and papain	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.jfoodeng.2008.08.002	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.jfoodeng.2008.08.002	en
heal.language	English	en
heal.publicationDate	2009	en
heal.abstract	Papain and ficin are general non-specific plant thiol proteases applied in food processing. Inactivation kinetics of papain and ficin were studied for thermal (50-80 degrees C, ambient pressure) and high pressure/temperature (500-900 MPa at 50-80 degrees C) process conditions. The effect of temperature at each pressure and the effect of pressure at each temperature were expressed by the values of activation energy. E-a, and activation volume, V-a The two enzymes showed the same inactivation under thermal process. At high pressures, at each process temperature, increase of pressure increases the inactivation rate. Up to 60 degrees C for ficin and 70 degrees C for papain, inactivation rates at high pressures are higher than the corresponding thermal rates at ambient pressure. At higher temperatures up to certain pressures an antagonistic effect was observed. At 80 degrees C thermal inactivation rates at all high pressures are lower than the ones at ambient pressure. E-a increased for papain (from 50 to 88 kJ/mol) and decreased for ficin (from 139 to 43 kJ/mol) as process pressure increased, a different effect of pressure on temperature sensitivity. V-a depended on process temperature showing increasing effect of pressure at higher temperatures for papain and decreasing for ficin. The enzymes inactivation rate constant was modeled as a function of both temperature and pressure conditions by a multi-parameter equation. Overall, papain and ficin showed a high thermal and pressure stability requiring intense process conditions for adequate inactivation. (C) 2008 Elsevier Ltd. All rights reserved.	en
heal.publisher	ELSEVIER SCI LTD	en
heal.journalName	Journal of Food Engineering	en
dc.identifier.doi	10.1016/j.jfoodeng.2008.08.002	en
dc.identifier.isi	ISI:000261895400006	en
dc.identifier.volume	91	en
dc.identifier.issue	1	en
dc.identifier.spage	42	en
dc.identifier.epage	48	en