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    A review on protein extracts from sunflower cake: techno-functional properties and promising modification methods
    (Taylor & Francis Inc, 2022) Gultekin Subasi, Busra; Vahapoglu, Beyza; Capanoglu, Esra; Mohammadifar, Mohammad Amin
    De-oiled sunflower cake is a sustainable and promising protein source with high phenolic and fiber contents. The cake, which is an industrial by-product has been the subject of many studies investigating various aspects such as protein extraction, functional properties, interaction with other ingredients, and its performance in a wide range of food products. Innovative and conventional techniques of protein extraction from sunflower cake have been investigated to increase extraction yield and improve desired functional characteristics. Modulation of structure of plant-based proteins helps to control their techno-functional properties and widen their applications. Structure modification of proteins by physical methods including ultrasound treatment and gamma irradiation as well as enzymatic and chemical methods has been used to improve the functional properties of sunflower protein. This review collects and critically discusses the available information on techno-functional properties of protein extracts from sunflower cake and how its techno-functional properties can be tailored using various structure modification methods.
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    Effect of moderate electric field on structural and thermo-physical properties of sunflower protein and sodium caseinate
    (Elsevier Sci Ltd, 2021) Subasi, Busra Gultekin; Jahromi, Mastaneh; Casanova, Federico; Capanoglu, Esra; Ajalloueian, Fatemeh; Mohammadifar, Mohammad Amin
    Moderate electric field (MEF) was employed to sunflower protein isolate (SPI) and sodium caseinate (CAS) to change their structural and thermo-physical properties with a non-thermal approach. MEF treatment significantly reduced the average particle size with noticeable changes in the uniformity of SPI and CAS solutions. A maximum of 10% reduction in the surface tension was observed for 0.2% w/w SPI sample by applying 150 V for 20 s. This effect was less pronounced for CAS samples and for the protein concentration of 2% w/w. FTIR spectra provided an increased ?-helix content for SPI inducing a bulkier, loosened and more hydrophilic structure which is unlikely for CAS. Intrinsic Fluorescence Spectroscopy revealed that MEF treatments changed the tertiary structures of SPI and CAS. Denaturation temperatures and enthalpies of the SPI and CAS samples were decreased by MEF treatments.
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    Influence of moderate electric field on sodium caseinate structure and its techno-functionality
    (Elsevier, 2022) Jahromi, Mastaneh; Niakousari, Mehrdad; Golmakani, Mohammad Taghi; Subasi, Busra Gultekin; Mohammadifar, Mohammad Amin
    This study aimed to evaluate the effect of moderate electric field (MEF) treatment, as a non-thermal technology, on the structure and techno-functionality of sodium caseinate. Colloidal dispersions of caseinate were subjected to different MEF processing conditions (2.56 V cm(-1) for 1 and 2 h, 38.46 V cm(-1) for 5 and 20 s) and their structural, physical, emulsifying and film-forming characteristics were assessed. The Fourier transform infrared (FTIR) analysis of the caseinate showed higher beta-structures and a reduction in random coil conformation after MEF. The MEF-treated dispersions exhibited smaller particle size and developed emulsions with higher physical stability. The process increased the tensile strength (by 6.52-27.37%) and stretchability (by 12.17-54.30%) of caseinate film. A higher glass transition temperature in MEF-processed caseinate films was confirmed by modulated differential scanning calorimetry (MDSC) profiles. The scanning electron microscope (SEM) images showed a more uniform microstructure in treated caseinate films. The results suggest that MEF may be efficiently applied for mild modification of the structure of caseinate resulting in its property improvement.
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    Influence of non-thermal microwave radiation on emulsifying properties of sunflower protein
    (Elsevier Sci Ltd, 2022) Subasi, Busra Gultekin; Yildirim-Elikoglu, Seda; Altay, Ipek; Jafarpour, Ali; Casanova, Federico; Mohammadifar, Mohammad Amin; Capanoglu, Esra
    Sunflower protein isolate obtained from industrially de-oiled press cake was treated with non-thermal microwave, aiming to investigate how structure and emulsifying properties were affected. Our results indicated that the content of polar amino acids was decreased and solubility and surface hydrophobicity were altered upon exposure to non-thermal microwave. Higher solubility and surface hydrophobicity of the samples treated with defrost mode and also 350 W were accompanied by a smaller size and lower uniformity of the oil droplets compared to the control and other samples. Non-thermal microwave treatment improved the emulsion stability by 1.43 times and defrost mode treated sample had the lowest stability index after 120 min. Interfacial dilatational rheology measurements revealed that 70 and 350 W treated samples created higher elastic, less stretchable solid-like layer at the O/W interface in comparison with defrost mode treated and control samples. Consequently, non-thermal microwave treatment could be considered as a promising simple, fast, and green protein modification technique.
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    Non-thermal Approach for Electromagnetic Field Exposure to Unfold Heat-Resistant Sunflower Protein
    (Springer, 2023) Subasi, Busra Gultekin; Yildirim-Elikoglu, Seda; Altin, Ozan; Erdogdu, Ferruh; Mohammadifar, Mohammad Amin; Capanoglu, Esra
    The non-thermal effect of electromagnetic field (NEF) on the structural and thermal properties of heat-resistant globular sunflower protein isolate was investigated by exposing samples to varying power levels (70 W, defrost (DF), and 350 W). Only the lowest consecutive power modes of the electromagnetic unit were conducted to complete at least two exposure cycles (for certainty) without exceeding 45 degrees C (non-thermal processing condition). The total polar amino acid content of the treated samples decreased by 14% with NEF applications since polar amino acids were the main targets of the electromagnetic field due to absorbing that energy as kinetic energy and inducing structural changes. The DF and 350 W treatments dissipated large particles/aggregates over 5000 nm completely. The treatment with the lowest power (70 W) produced the lowest average particle size (14% decrease) while it increased after the DF and 350 W applications (34 and 16%, respectively), which indicated partial unfolding and/or reaggregation. Less ordered structures had increased alpha-helix (max with 350 W by 22%) and decreased beta-sheet contents (max with 70 W by 30%) after the NEF treatments. The tertiary structures of the samples changed significantly following the NEF treatments with a blue shift on emission maxima with different fluorescence intensities. The thermal stability of the samples was analyzed with DSC and TGA; lower peak temperature (decreased by 28%) and denaturation enthalpy (decreased by 82%) besides higher gravimetric loss (by 1.3%) were obtained for DF and 350 W, compared to the control. The NEF could be considered a promising approach for structural alteration of globular sunflower protein.
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    Protein extracts from de-oiled sunflower cake: Structural, physico-chemical and functional properties after removal of phenolics
    (Elsevier, 2020) Subasi, Busra Gultekin; Casanova, Federico; Capanoglu, Esra; Ajalloueian, Fatemeh; Sloth, Jens J.; Mohammadifar, Mohammad Amin
    The effects of dephenolization on structural, physico-chemical and functional properties of sunflower protein isolate obtained from de-oiled sunflower cake were investigated. Proximate analysis showed that the moisture and crude protein content for sunflower dephenolized protein (SPI-DP) increased by 59 and 9% compared to the natural sunflower protein (SPI-N) samples, while the ash content and phenolic compounds decreased 53 and 98%, respectively. Powder of SPI-DP had a yellowish color and analysis using scanning electron microscopy showed a rough and spongy surface compared to SPI-N. The isoelectric point of SPI-N and SPI-DP were observed at pH 4.37 and 4.82, respectively. Analysis of mineral composition showed a lowered amount of minerals (except for Se and Sr), as a result of phenolic removal. Secondary structures of the protein did not change but lower hydrophilicity was observed after phenolic removal using Fourier transform infrared spectroscopy. No difference was observed using differential scanning calorimetry on the glass transition and denaturation temperatures. Higher values for foam capacity and foam stability were observed for SPI-DP compared to SPI-N. Interfacial rheological measurements showed that structure strength at the air/water interface increased after phenolic removal.