Food Engineering / Gıda Mühendisliği

Permanent URI for this collectionhttps://hdl.handle.net/11147/12

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  • Article
    Citation - WoS: 49
    Citation - Scopus: 66
    Bioactive, Functional and Edible Film-Forming Properties of Isolated Hazelnut (corylus Avellana L.) Meal Proteins
    (Elsevier Ltd., 2014) Aydemir, Levent Yurdaer; Adan Gökbulut, Aysun; Baran, Yusuf; Yemenicioğlu, Ahmet
    This study aimed characterization of bioactive, functional and edible film making properties of isolated proteins from untreated (HPI), hot extracted (HPI-H), acetone washed (HPI-AW), and acetone washed and hot extracted (HPC-AW-H) hazelnut meals. The most bioactive protein extract was HPC-AW-H, followed by HPI-AW, HPI-H and HPI, based on antioxidant activity (TEAC and ORAC: 158-461mmolTrolox/kg), iron chelation (60.7-126.7mmolEDTA/kg), angiotensin-converting enzyme inhibition (IC50: 0.57-1.0mg/mL) and antiproliferative activity on colon cancer cells (IC50: 3.0-4.6mg/ml). Protein contents of HPI, HPI-H and HPI-AW (93.3-94.5%) were higher than that of HPC-AW-H (86.0%), but HPC-AW-H showed the best pH-solubility profile. The extracts showed good oil absorption (7.4-9.4g/g) and foaming, but limited water holding and gelling capacities, and emulsion stability. The protein extracts gave transparent, yellowish to brownish and reddish colored and water soluble edible films. The HPI gave the lightest colored films with acceptable mechanical properties (elongation up to 144% and tensile strength up to 4.9MPa). 1-D and 2-D electrophoresis clearly showed the molecular and isoelectric profiles of hazelnut proteins. The overall results of this study showed that the bioactive, solubility and gelation properties of hazelnut proteins could be improved by simple processes like acetone washing and/or heat treatment. The hazelnut proteins are valuable as multipurpose food ingredients.
  • Article
    Citation - WoS: 104
    Citation - Scopus: 123
    Potential of Turkish Kabuli Type Chickpea and Green and Red Lentil Cultivars as Source of Soy and Animal Origin Functional Protein Alternatives
    (Academic Press Inc., 2013) Aydemir, Levent Yurdaer; Yemenicioğlu, Ahmet
    In this study, functional properties of proteins from Turkish Kabuli type chickpea (CPEs) and green and red lentil cultivars (LPEs) were characterized and compared with those of soy and animal proteins. The LPEs and whey protein isolate (WPI) showed higher soluble and total protein content than the other proteins. CPEs showed the highest oil absorption capacity (10.9-14.59 g/g), followed by LPEs (6.90 -10.44 g/g), soy protein extract (8.23 g/g), and egg white proteins (6.37 g/g). The highest water absorption capacities were obtained for bovine gelatin (BGEL) (8.84 g/g), CPEs (4.90-7.94 g/g) and soy protein isolate (7.94 g/g). The foaming capacities of BGEL and fish gelatin (FGEL), and emulsifying capacity of WPI were slightly higher than those of CPEs and LPEs, but most stable emulsions and foams were formed by chickpea and lentil proteins. The least gelling concentration of CPEs (5-7 g/100 g) came second after BGEL (3 g/100 g). The 2-D electrophoresis revealed the detailed isoelectric point (between 4.5 and 5.9) and molecular weight patterns of chickpea and lentil proteins. This study clearly showed that the functional properties of Kabuli chickpea proteins are superior than those of lentil proteins and most of the studied soy and animal proteins.
  • Article
    Citation - WoS: 98
    Citation - Scopus: 118
    Antioxidant Activity of Protein Extracts From Heat-Treated or Thermally Processed Chickpeas and White Beans
    (Elsevier Ltd., 2007) Arcan, İskender; Yemenicioğlu, Ahmet
    In this study, antioxidant activities of water-soluble protein extracts from chickpeas and white beans were investigated. The area under the curve (AUC) values of lyophilized crude protein extracts (dialyzed or undialyzed) from thermally processed (121 °C for 20 min) or heat-treated (90 °C for 20 min) chickpeas (73-91 μmol trolox/g) and white beans (39-67 μmol trolox/g) indicated a higher free radical-scavenging capacity and thermostability for chickpea proteins than for white bean proteins. The thermal processing also increased the Fe+2-chelating capacity of lyophilized chickpea crude protein extracts 1.8-fold whereas it caused a 2.3-fold reduction in the Fe+2-chelating capacity of lyophilized white bean crude protein extracts. Dialysis increased the protein content of lyophilized chickpea extracts 1.5-2-fold but it did not affect the protein content of lyophilized white bean extracts significantly. Ammonium sulfate precipitation was not effective for selective precipitation of antioxidant proteins. However, it improved the free radical-scavenging capacity of lyophilized protein extracts from thermally processed chickpeas and white beans by almost 25% and 100%, respectively. DEAE-cellulose chromatography, indicated the presence of five (A1-A5) and three (B1-B3) antioxidant protein fractions in heat-treated and thermally processed chickpea protein extracts, respectively, and can be used for the partial purification of antioxidant proteins. The results of this study showed the good potential of chickpea proteins as thermostable natural food antioxidants.