caa a22 4500 510725511 CHVBK 20190416140728.0 cr unu---uuuuu 180411e20131201xx s 000 0 eng 10.1007/s11947-012-0984-5 doi (NATIONALLICENCE)springer-10.1007/s11947-012-0984-5 Thermal and High-Pressure Stability of Pectinmethylesterase, Polygalacturonase, β-Galactosidase and α-Arabinofuranosidase in a Tomato Matrix: Towards the Creation of Specific Endogenous Enzyme Populations Through Processing [Elektronische Daten] [Ken Houben, Zahra Jamsazzadeh Kermani, Sandy Van Buggenhout, Ruben Jolie, Ann Van Loey, Marc Hendrickx] The thermal and pressure stability of tomato pectinmethylesterase (PME), polygalacturonase (PG), β-galactosidase (β-Gal), and α-arabinofuranosidase (α-Af) were investigated in situ. Enzyme inactivation by thermal and high-pressure processing (respectively 5min at 25-95°C at 0.1MPa and 10min at 0.1-800MPa at 20°C) was monitored by measuring the residual activity in crude enzyme extracts of treated tomato purée samples. PME was completely inactivated after a 5-min treatment at 75°C. Only 30% of the pressure stable PME was inactivated after a treatment at 800MPa (20°C, 10min). A 5-min treatment at 95°C and a treatment at 550MPa (20°C, 10min) caused complete PG inactivation. β-Gal and α-Af activities were already reduced significantly by thermal treatments at 42.5-52.5°C and 45-60°C, respectively. These enzymes were, however, rather pressure resistant: treatments at respectively 700 and 600MPa were necessary to reduce the activity below 10% of the initial value. Assuming that first-order, fractional conversion or biphasic inactivation models could be applied to the respective enzyme inactivation data, inactivation rate constants and their temperature or pressure dependence for the different enzymes were determined. Based on differences in process stability of the enzymes, possibilities for the creation of specific "enzyme populations” in tomato purée by selective enzyme inactivation were identified. For industrially relevant process conditions, the enzyme inactivation data obtained for tomato purée were shown to be transferable to intact tomato tissue. Springer Science+Business Media New York, 2012 Tomato nationallicence Structure nationallicence Pectinmethylesterase nationallicence Polygalacturonase nationallicence β-Galactosidase nationallicence α-Arabinofuranosidase nationallicence Houben Ken Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Jamsazzadeh Kermani Zahra Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Van Buggenhout Sandy Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Jolie Ruben Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Van Loey Ann Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Hendrickx Marc Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut Food and Bioprocess Technology Springer US; http://www.springer-ny.com 6/12(2013-12-01), 3368-3380 1935-5130 6:12<3368 2013 6 11947 https://doi.org/10.1007/s11947-012-0984-5 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11947-012-0984-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Houben Ken Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 700 1- Jamsazzadeh Kermani Zahra Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 700 1- Van Buggenhout Sandy Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 700 1- Jolie Ruben Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 700 1- Van Loey Ann Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 700 1- Hendrickx Marc Department of Microbial and Molecular Systems (M2S), Laboratory of Food Technology and Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 22, PB 2457, 3001, Leuven, Belgium aut NATIONALLICENCE 773 0- Food and Bioprocess Technology Springer US; http://www.springer-ny.com 6/12(2013-12-01), 3368-3380 1935-5130 6:12<3368 2013 6 11947 Metadata rights reserved Springer special CC-BY-NC licence nationallicence SWISSBIB 510725511 BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer