dc.contributor.author | Tijskens, LMM | en |
dc.contributor.author | Rodis, PS | en |
dc.date.accessioned | 2014-06-06T06:43:24Z | |
dc.date.available | 2014-06-06T06:43:24Z | |
dc.date.issued | 1997 | en |
dc.identifier.issn | 13309862 | en |
dc.identifier.uri | http://62.217.125.90/xmlui/handle/123456789/1241 | |
dc.relation.uri | http://www.scopus.com/inward/record.url?eid=2-s2.0-0002968883&partnerID=40&md5=fe4fa536efa658cd1138b971a441a0fe | en |
dc.subject | Apparent activity | en |
dc.subject | Enzyme denaturation | en |
dc.subject | Generic model | en |
dc.subject | Kinetics | en |
dc.subject | Peaches | en |
dc.subject | Processing | en |
dc.subject | Storage | en |
dc.title | Kinetics of enzyme activity in peaches during storage and processing | en |
heal.type | conferenceItem | en |
heal.publicationDate | 1997 | en |
heal.abstract | The behaviour and activity of the enzymes polygalacturonase (PG, endo- EC. 3.2.1.15 and exo- EC. 3.2.1.67) and of pectin methyl esterase (PE, EC. 3.1.1.11) in peaches, measured during storage and processing, was modelled, based on the fundamental laws of kinetics. For both enzymes the activity was susceptible to senescence (PG) or denaturation (PE) counteracting a formation out of precursor or a bound and inactive form of the enzyme. For PE the behaviour was clearly based on two isoenzymes with, at a certain temperature, a conversion between the two configurations. | en |
heal.journalName | Food Technology and Biotechnology | en |
dc.identifier.issue | 1 | en |
dc.identifier.volume | 35 | en |
dc.identifier.spage | 45 | en |
dc.identifier.epage | 50 | en |
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