Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/2135
Full metadata record
DC FieldValueLanguage
dc.contributor.authorTarı, Canan-
dc.contributor.authorDoğan, Nergiz-
dc.contributor.authorGöğüş, Nihan-
dc.date.accessioned2016-09-02T13:30:20Z
dc.date.available2016-09-02T13:30:20Z
dc.date.issued2008-12-15
dc.identifier.citationTarı, C., Doğan, N., and Göğüş, N. (2008). Biochemical and thermal characterization of crude exo-polygalacturonase produced by Aspergillus sojae. Food Chemistry, 111(4), 824-829. doi:10.1016/j.foodchem.2008.04.056en_US
dc.identifier.issn0308-8146
dc.identifier.issn0308-8146-
dc.identifier.urihttp://doi.org/10.1016/j.foodchem.2008.04.056
dc.identifier.urihttp://hdl.handle.net/11147/2135
dc.description.abstractCrude exo-polygalacturonase enzyme (produced by Aspergillus sojae), significant for industrial processes, was characterized with respect to its biochemical and thermal properties. The optimum pH and temperature for maximum crude exo-polygalacturonase activity were pH 5 and 55 °C, respectively. It retained 60-70% of its activity over a broad pH range and 80% of its initial activity at 65 °C for 1 h. The thermal stability study indicated an inactivation energy of Ed = 152 kJ mol-1. The half lives at 75 and 85 °C were estimated as 3.6 and 1.02 h, respectively. Thermodynamic parameters, ΔH*, ΔS* and ΔG*, were determined as a function of temperature. The kinetic constants Km and Vmax, using polygalacturonic acid as substrate, were determined as 0.424 g l-1 and 80 μmol min-1, respectively. SDS-PAGE profiling revealed three major bands with molecular weights of 36, 53 and 68 kDa. This enzyme can be considered as a potential candidate in various applications of waste treatment, in food, paper and textile industries.en_US
dc.description.sponsorshipİYTEen_US
dc.language.isoenen_US
dc.publisherElsevier Ltd.en_US
dc.relation.ispartofFood Chemistryen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAspergillus sojaeen_US
dc.subjectBiochemical and thermal propertiesen_US
dc.subjectEnzyme characterizationen_US
dc.subjectMicrobial enzymesen_US
dc.subjectPolygalacturonaseen_US
dc.titleBiochemical and thermal characterization of crude exo-polygalacturonase produced by Aspergillus sojaeen_US
dc.typeArticleen_US
dc.authoridTR41331en_US
dc.authoridTR130613en_US
dc.institutionauthorTarı, Canan-
dc.institutionauthorDoğan, Nergiz-
dc.institutionauthorGöğüş, Nihan-
dc.departmentİzmir Institute of Technology. Food Engineeringen_US
dc.identifier.volume111en_US
dc.identifier.issue4en_US
dc.identifier.startpage824en_US
dc.identifier.endpage829en_US
dc.identifier.wosWOS:000258369600004en_US
dc.identifier.scopus2-s2.0-46949092740en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1016/j.foodchem.2008.04.056-
dc.relation.doi10.1016/j.foodchem.2008.04.056en_US
dc.coverage.doi10.1016/j.foodchem.2008.04.056en_US
local.message.claim2022-06-03T15:11:59.234+0300*
local.message.claim|rp02310*
local.message.claim|submit_approve*
local.message.claim|dc_contributor_author*
local.message.claim|None*
dc.identifier.wosqualityQ1-
dc.identifier.scopusqualityQ1-
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeArticle-
crisitem.author.dept03.08. Department of Food Engineering-
Appears in Collections:Food Engineering / Gıda Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
Files in This Item:
File Description SizeFormat 
2135.pdfMakale299.63 kBAdobe PDFThumbnail
View/Open
Show simple item record



CORE Recommender

SCOPUSTM   
Citations

51
checked on Nov 15, 2024

WEB OF SCIENCETM
Citations

43
checked on Nov 16, 2024

Page view(s)

308
checked on Nov 18, 2024

Download(s)

750
checked on Nov 18, 2024

Google ScholarTM

Check




Altmetric


Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.