Modeling the effect of temperature and high hydrostatic pressure on the proteolytic activity of kiwi fruit juice

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	2014-03-01T01:31:14Z
dc.date.available	2014-03-01T01:31:14Z
dc.date.issued	2009	en
dc.identifier.issn	0260-8774	en
dc.identifier.uri	https://dspace.lib.ntua.gr/xmlui/handle/123456789/19753
dc.subject	Actinidin	en
dc.subject	Enzyme kinetics	en
dc.subject	High pressure	en
dc.subject	Proteolytic activity	en
dc.subject	Thermal inactivation	en
dc.subject.classification	Engineering, Chemical	en
dc.subject.classification	Food Science & Technology	en
dc.subject.other	Actinidin	en
dc.subject.other	Activation energy e	en
dc.subject.other	Activation volumes	en
dc.subject.other	Effect of temperatures	en
dc.subject.other	Enzyme inactivations	en
dc.subject.other	First-order kinetics	en
dc.subject.other	Food industries	en
dc.subject.other	Function of pressures	en
dc.subject.other	High hydrostatic pressures	en
dc.subject.other	High pressure	en
dc.subject.other	Kiwi fruits	en
dc.subject.other	Milk-clotting enzymes	en
dc.subject.other	Moderate temperatures	en
dc.subject.other	Multi parameters	en
dc.subject.other	Pressure domains	en
dc.subject.other	Process conditions	en
dc.subject.other	Processing conditions	en
dc.subject.other	Proteolytic activity	en
dc.subject.other	Sulfhydryl	en
dc.subject.other	Thermal inactivation	en
dc.subject.other	Actinides	en
dc.subject.other	Activation energy	en
dc.subject.other	Amines	en
dc.subject.other	Chromophores	en
dc.subject.other	Dairy products	en
dc.subject.other	Enzyme kinetics	en
dc.subject.other	Enzymes	en
dc.subject.other	Fruit juices	en
dc.subject.other	Fruits	en
dc.subject.other	Hydraulics	en
dc.subject.other	Hydrodynamics	en
dc.subject.other	Hydrostatic pressure	en
dc.subject.other	Pressure effects	en
dc.subject.other	Proteolysis	en
dc.subject.other	Stainless steel	en
dc.subject.other	Thermal effects	en
dc.subject.other	Enzyme activity	en
dc.subject.other	Actinidia deliciosa	en
dc.title	Modeling the effect of temperature and high hydrostatic pressure on the proteolytic activity of kiwi fruit juice	en
heal.type	journalArticle	en
heal.identifier.primary	10.1016/j.jfoodeng.2009.02.026	en
heal.identifier.secondary	http://dx.doi.org/10.1016/j.jfoodeng.2009.02.026	en
heal.language	English	en
heal.publicationDate	2009	en
heal.abstract	Actinidin is the sulfhydryl protease of kiwi fruit. It can have applications in the food industry replacing other plant sulfhydryl proteases like papain and ficin, as milk clotting enzyme for traditional and novel dairy products, as meat tenderizer and beer clarifier. High hydrostatic pressure (HHP) will allow the controlled inactivation of actinidin after it has been applied and caused the desirable extent of clotting or tenderization, respectively. Thermal inactivation and inactivation by HHP (200-800 MPa) combined with moderate temperature (25-50 degrees C) of the endogenous actinidin in kiwi fruit juice was studied. The enzyme activity was measured spectrophotometrically based on the hydrolysis of a chromophore-peptide compound. Actinidin inactivation followed first order kinetics at the studied processing conditions. The activation energy E, and the activation volume V-a were expressed as a function of pressure and temperature, respectively. The enzyme inactivation was modeled by a single multi-parameter equation in the studied temperature and pressure domain. The developed kinetics allow the selection of optimal HHP process conditions for achieving the desirable enzyme activity control after the targeted proteolysis has been achieved in products where the kiwi fruit actinidin has been applied. (C) 2009 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.2009.02.026	en
dc.identifier.isi	ISI:000266737800007	en
dc.identifier.volume	94	en
dc.identifier.issue	1	en
dc.identifier.spage	40	en
dc.identifier.epage	45	en