Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/4237
Full metadata record
DC FieldValueLanguage
dc.contributor.advisorYemenicioğlu, Ahmet-
dc.contributor.authorAydemir, Levent Yurdaer-
dc.date.accessioned2014-12-04T14:42:37Z-
dc.date.available2014-12-04T14:42:37Z-
dc.date.issued2014-07-
dc.identifier.urihttp://hdl.handle.net/11147/4237-
dc.descriptionThesis (Doctoral)--Izmir Institute of Technology, Food Engineering, Izmir, 2014en_US
dc.descriptionIncludes bibliographical references (leaves: 114-128)en_US
dc.descriptionText in English; Abstract: Turkish and Englishen_US
dc.descriptionFull text release delayed at author's request until 2017.08.08en_US
dc.description.abstractIn this thesis, technological and bioactive properties of protein concentrates and isolates form Turkish lentil and chickpea cultivars and hazelnut meal has been characterized. This study aimed to increase industrially suitable alternatives to soy and animal origin proteins. The functional properties (solubility, gelation, water and oil absorption, emulsion and foaming capacity and stability) of globulin proteins from chickpeas are comparable or superior than those of soy proteins and most animal proteins (fish and bovine gelatin, egg white and whey proteins) with the exception of gelation capacity of bovine gelatin. The chickpea proteins got extremely high water (4.9-7.9 g/g) and oil (10.9-14.6 g/g) absorption capacity. The lentil globulins showed high protein solubility (0.56-0.69 g/g) and oil absorption capacities (6.9-10.4 g/g), but missed water absorption and gelation properties. The lentil proteins showed 2-3 fold higher antioxidant capacity than the chickpea proteins, and antioxidant lentil protein fractions could be separated or concentrated by isoelectric precipitation, ion exchange chromatography and ultrafiltration. The hazelnut meal globulins showed satisfactory oil absorption (7.4-9.4 g/g) and good foaming (7.1 to 18.9 ml foam with 10 mg/ml), but poor water absorption, gelation and emulsion properties. The hazelnut proteins also form water soluble yellowish to brownish and reddish colored transparent edible films with 10-12.5 % (w/w) solutions. However, the most outstanding properties of hazelnut meal proteins is their high bioactivity including free radical scavenging (158-461 μmol Trolox/g), iron chelation (60.7-126.7 μmol EDTA/g) and angiotensin-converting enzyme inhibition (IC50: 0.57-1.0 mg/mL) capacities. Thus, a functional beverage, hazelnut milk enriched with trypsin and pepsin hydrolyzed hazelnut globulins, was developed as an example functional food product. This work showed the good potential of selected Turkish plant resources as animal and soy protein alternatives.en_US
dc.language.isoenen_US
dc.publisherIzmir Institute of Technologyen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectFunctional foodsen_US
dc.subjectPlant based proteinsen_US
dc.subjectFunctional properties of proteinsen_US
dc.subjectAntioxidanten_US
dc.titleProduction of high quality functional proteins from legumes and plant based agroindustrial wastes and byproductsen_US
dc.title.alternativeBaklagiller ve bitkisel kaynaklı tarımsal atıklar ve yan ürünlerinden yüksek kalitede fonksiyonel proteinler üretilmesien_US
dc.typeDoctoral Thesisen_US
dc.authorid0000-0003-0372-1172en_US
dc.departmentThesis (Doctoral)--İzmir Institute of Technology, Food Engineeringen_US
dc.relation.publicationcategoryTezen_US
item.fulltextWith Fulltext-
item.grantfulltextopen-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.openairetypeDoctoral Thesis-
Appears in Collections:Phd Degree / Doktora
Files in This Item:
File Description SizeFormat 
10013321.pdfDoctoralThesis2.46 MBAdobe PDFThumbnail
View/Open
Show simple item record



CORE Recommender

Page view(s)

214
checked on Nov 18, 2024

Download(s)

114
checked on Nov 18, 2024

Google ScholarTM

Check





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