Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7148

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  • Article
    Automated Detection and Quantification of Honey Adulteration Using Thermal Imaging and Convolutional Neural Networks
    (Pergamon-Elsevier Science Ltd, 2026) Unluturk, Mehmet S.; Berk, Berkay; Unluturk, Sevcan
    Honey is a valuable natural food rich in bioactive substances beneficial to health. Despite strict regulations prohibiting adulteration, honey remains one of the most frequently adulterated foods, often with low-cost commercial syrups. Conventional detection methods require expensive instruments, expert operators, and lengthy analysis times, limiting their practical use. This study introduces a rapid and automated method for detecting and quantifying honey adulteration using thermal image analysis combined with a tailored Convolutional Neural Network (CNN) architecture. Thirty-six pure honey samples (blossom and honeydew) from different regions of T & uuml;rkiye were adulterated with inverted sugar, maltose, and glucose syrups at varying levels (3 %-60 % weight/weight (w/w)). Samples were heated to 60 degrees C and thermal images were captured during cooling using a custom image-capturing unit. The CNN model employed a multi-layer structure, starting with a shallow network for binary classification (pure vs adulterated honey) achieving 100 % accuracy, followed by specialized deeper CNN regressors to quantify adulterant levels with mean squared errors of 0.0003, 0.001, and 0.0002 for glucose, maltose, and inverted sugar, respectively. This layered CNN approach leverages thermal patterns linked to adulteration, enabling sensitive, rapid, and non-destructive quality control. Furthermore, the method is integrated into a user-friendly hardware-software system called Compact Adulteration Testing Cabinet on Honey (CATCH), requiring no specialized expertise, demonstrating strong potential for automated honey authenticity verification in practical settings.
  • Article
    Harnessing Pulse Proteins as Soy Protein Substitutes in Spreadable Cheese Analogues: Exploring Correlations Among Protein Techno-Functionality, and Cheese Textural, Rheological and Sensory Properties
    (Elsevier Sci Ltd, 2026) Cavdaroglu, Elif; Topcuoglu, Meryem; Acar, Eda; Polat, Nil Yaren; Berk, Berkay; Cavdaroglu, Cagri; Yemenicioglu, Ahmet
    This study aimed at comparing techno-functional properties of faba bean (FBP), pinto bean (PBP), cowpea (CPP) and mung bean (MBP) proteins with commercial soy protein isolate (SPI), and exploring their correlations with textural, rheological and sensory properties of plant protein-based spreadable cheese analogues. FBP and MBP showed the best solubility between pH 3.0 and 11.0. The highest and the lowest water and oil (OAC) absorption capacities were observed for SPI and MBP (7.78 and 0.79 g H2O/g), and PBP and SPI (7.79 and 3.55 g oil/g). Protein's least gelling concentrations (LGC) ranged from 10 % (SPI) to 18 % (FBP). CPP, MBP, and PBP formed harder, gummier gels at >= LGC than SPI and FBP. Pre-gels of PBP and CPP at <= LGCs showed the highest consistency and viscosity indexes. Proteins showed similar emulsification. Cheese analogue from SPI (SPIC) showed the highest firmness (37.5 N) and work to shear for spreadability (57.5 N s), followed by cheese analogues of other proteins such as MBPC, CPPC, FBPC, and PBPC in descending order. The highest and lowest elastic (G ') and viscous (G '') moduli were obtained for MBPC (G' = 4353 and G"= 1277) and PBPC (G' = 377 Pa and G"= 98 Pa). OAC of proteins correlated with cheese analogues' firmness (r =- 0.918), work to shear for spreadability (r =- 0.910), and stickiness (r =- 0.894). Tan delta (G"/G ') of cheese analogues correlated with work to shear for spreadability (r = 0.986). SPIC and FBPC received the highest overall liking scores correlated mainly with appearance, color and taste. Correlating protein techno-functionality in cheese analogue opens new horizons for effective utilization of pulse proteins as soy protein substitutes.