67 research outputs found

    Comparative review of three approaches to biofuel production from energy crops as feedstock in a developing country

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    This study is a comparative evaluation of three approaches to biofuel production from energy crops including biogas, bioethanol and biodiesel to ascertain which one is the most effective and more energy-efficient than the others. Moreover, the potential of biofuel production from the best option was studied. For this purpose, biogas generation from corn silage, bioethanol generation from corn, and biodiesel production from peanuts in Iran (as a case study) were studied. The results revealed that 10,683.36 m3 of biogas, 2.53 m3 of bioethanol and 0.70 m3 of biodiesel could be produced per each hectare of energy crops. The total greenhouse gas emissions for each MJ energy generation of biogas, bioethanol and biodiesel were 0.01, 0.04 and 0.03 kgCO2eq, respectively. Accordingly, the total annual biogas potential from corn silage (as the best option) in Iran is 3953.74 million m3, which is equivalent to 1515.94 million barrels of oil

    Aggregability and digestibility study of fruit juice fortified camel milk powder proteins

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    In this work, we observed the effect of grape juice (% concentrated juice/% concentrated camel milk: GJ20/80, GJ50/50) and pomegranate juice (PJ20/80, PJ40/60) fortification on camel milk (CM) protein solubility and digestibility. Proteins were dissolved in sodium phosphate buffer to 50 mg/ml and defatted prior Bradford assay of protein concentration, then analyzed by Size Exclusion-Ultra High-Performance Liquid chromatography (SE-UHPLC). The CM protein aggregation and their stability were further monitored at different pH 2.0, 4.0, and 7.5 via sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Freeze dried CM (FDCM) was the reference sample and our results showed that GJ50/50 and PJ40/60 with the highest fruit juice ratio had the lowest protein content in the supernatant, hence the decreased solubility. SE-UHPLC of supernatants showed a slight decrease in retention times of 11 kDa and 62 kDa proteins for GJ50/50 and PJ40/60 suggesting a possibility of adduct formation due to fortification leading to higher molecular weight. The simulated static in vitro gastrointestinal digestion of samples revealed that most soluble proteins were readily digested by pepsin, trypsin and chymotrypsin enzymes leading to small peptides. However, the SDS PAGE of pellets showed the partial resistance of casein and α-lactalbumin against peptic digestion.Supplementary material: [https://cherry.chem.bg.ac.rs/handle/123456789/4747

    Dietary fiber components, microstructure, and texture of date fruits (Phoenix dactylifera, L.)

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    Date fruits vary widely in the hardness of their edible parts and they are classifed accordingly into soft, semi-dry, and dry varieties. Fruit texture, a signifcant parameter in determining consumer acceptance, is related to the tissue structure and chemical composition of the fruit, mainly the ratio of sucrose to reducing sugars. This study aimed to understand the relationship between the chemical composition, microstructure, and texture profle of 10 major Emirati date fruits. The soluble sugars, glucose and fructose, represent ca 80 g/100 g of the fruits on the basis of dry weight (DW) while the dietary fber contents varied 5.2–7.4 g/100 dg D.W. with lignin being the main determinant of the variability. The textures of the samples were studied using instrumental texture profle analysis. While no correlation was found between the soluble sugar and texture parameters in this study, the diferent fber constituents correlated variably with the diferent parameters of date fruit texture. Lignin, arabinoxylan, galactomannan, and pectin were found to correlate signifcantly with fruit hardness and the related parameters, gumminess and chewiness. Both lignin and arabinoxylan correlated with resilience, and arabinoxylan exhibited a strong correlation with cohesiveness

    Spray drying of camel milk induces protein aggregates and Maillard reaction products formation

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    Camel milk (CM) powders are nutritious food with many health benefits. We investigated physicochemical properties of CM proteins upon spray drying at six inlet temperatures (190°C - 250°C). Electrophoretic and spectrophotometric analysis revealed occurrence of Maillard reaction upon spray drying. Size exclusion chromatography showed increase in protein Mw and aggregates formation. Spray drying inlet temperatures exerted significant effects on the properties of CM powder proteins. Project was supported by the GA No.172024 of Ministry of Education, Science and Technological Development

    Correction to: Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source (Sci Rep 2021, 11 (1), 14030. DOI: https://doi.org/10.1038/s41598-021-93284-8)

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    In the original version of this Article, Sam Van Haute and Sami Ghnimi were omitted as corresponding authors. Correspondence and requests for materials should also be addressed to [email protected] and sghnimi@ isara.fr. The original Article has been corrected.The contribution corrects an equation from the paper: Nikkhah, A.; Van Haute, S.; Jovanović, V.; Jung, H.; Dewulf, J.; Ćirković-Veličković, T.; Ghnimi, S. Life Cycle Assessment of Edible Insects (Protaetia Brevitarsis Seulensis Larvae) as a Future Protein and Fat Source, Sci Rep 2021, 11 (1), 14030.[https://doi.org/10.1038/S41598-021-93284-8]Link to the corrected article: [https://cherry.chem.bg.ac.rs/handle/123456789/4584

    Electrophoretic and mass spectrometry-based characterization of soluble fraction of camel milk proteins upon freeze and spray drying treatment

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    Objective: Camel milk is highly nutritious food with numerous health benefits proposed. Demand for camel milk has increased worldwide.Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we characterized proteins of soluble fraction of freeze/spray dried camel milk powders. Material and Methods: Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic techniques and circular dichroism. Freeze dried camel milk and spray dried at 250°C were analysed by mass spectrometry. Results: SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated occurence of the Maillard reaction. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Mass spectrometry identified α-lactalbumin, glycosylation-dependant cell adhesion molecule 1 (GLYCAM1), immunoglobulin heavy chain, peptidoglycan recognition protein and camel serum albumin as dominant proteins in soluble fraction of camel milk powders. Carboxymethyl-lisyne (CML), well known marker of Maillard reaction in food analysis, was detected on GLYCAM1 and on immunoglobulin heavy chain. Conclusions: Our results indicate glycation of camel milk proteins via Maillard reaction upon spray drying treatment which further may affect techno-functional properties of camel milk powders, their shelf-life and nutritional value. Acknowledgments: This work was supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, grant number 172024. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752

    Physicochemical characterization of soluble proteins of whole camel milk powders produced by spray drying treatment at high temperatures

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    Objective. Camel milk is highly nutritious food with numerous health benefits proposed. Demand for camel milk has increased worldwide. Production of camel milk powders facilitate its transport, prolonge shelf-life, and also offer an attractive additive for various food products. In this study we characterized proteins of soluble fraction of freeze/spray dried camel milk powders. Material and Methods. Whole camel milk powders were prepared by spray drying treatment at six different inlet temperatures (190°C - 250°C) or by freeze drying. The soluble protein fractions upon the treatments were analysed by combination of electrophoretic and spectroscopic techniques. Functional properties, such as antioxidant activity and protein solubility were assessed. Results. SDS-PAGE revealed non-uniform increase in Mw of major protein bands, while native electrophoresis revealed non-uniform decrease in pI values with increased inlet temperature of spray drying. That indicated attachement of lactose moieties to NH2- group of proteins via non-enzymatic Maillard reaction. Spectrophotometric analysis showed formation of intermediate Maillard reaction products (increased absorbance at 294 nm) and no detectable late Maillard reaction products formation. Far-UV circular dichroism spectra showed no differences in secondary structures between freeze and spray dried samples. Antioxidant activity and protein solubility were increased with increase in inlet temperature. Conclusions. Our results showed that spray drying treatment promoted non-enzymatic glycation of camel milk proteins. Glycation of food proteins affects their technofunctional properties, shelf-life and nutritional value. Thus, optimization of spray drying parametars is essential for production of high quality camel milk powders. Acknowledgements: This research work was funded the Ministry of Education and Science of the Republic of Serbia, GA No. OI172024, Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718, Serbian Academy of Sciences and Arts Project F-26. The project leading to this application has received funding from the European Union's Horizon 2020 research and innovation programme under grant agreement No 810752
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