@conference{
author = "Jovanović, Vesna and Radomirović, Mirjana Ž. and Krstić-Ristivojević, Maja and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "In the last several decades, the trend of seafood consumption has significantly increased not only in the countries with a tradition of seafood consumption, but also in other ones [1]. The increase in the world's population and the awareness of healthy food, the globalization of markets, and the development of aquaculture are some of the factors that have led to this trend. The aquaculture of shellfish like clams, mussels, oysters and scallops has been very developed all around the world and the food products based on them have become part of the daily diet for many consumers. In addition, these food products are considered healthy food because of the high content of proteins and essential fatty acids, but their consumption may carry some risks of food allergy. Tropomyosin from shellfish (TPM) is the major allergen responsible for the development of anaphylaxis in persons with food allergy. The content of TPM in shellfish and its bioavailability from food products can have potential influence on the sensitization of consumers to TPM. It is known that food processing can change the bioavailability of food allergens [2]. The main goal of this study was the investigation of how processing and packaging of shellfish samples can affect the content of TPM in them.
For this study, clam Venerupis philippinarum was chosen as the species with the highest world aquaculture production [1]. After the purchasing of live clams, the animals were separated into 5 groups for the next treatments: fresh live (control group), freshly removed inner content was kept at +4°C for 3 days (three days` shelf-life), frozen in a plastic bag and kept at -20 °C during 7 days, marinated and kept in a glass jar at room temperature during 8 days and freshly boiled. After processing and packaging of samples, the total protein extracts were prepared in 10 mM sodium phosphate buffer pH 7.4 1M NaCl, 1 mM PMSF and the concentration of total proteins was determined by BCA method. The concentration of TPM in the total protein extracts was determined using a sandwich Enzyme-Linked Immunosorbent Assay (ELISA) using in-house prepared clams` TPM standard. The content of TPM (μg) in the samples was expressed per mg of extracted soluble proteins, individual animal and grams of soft wet tissue.
The cooked samples have significantly higher TPM content expressed per gram of soft wet tissue compared to all other treatments. Food processing such as freezing, marinating, or extending the shelf-life at 4°C by 3 days has very little effect on the change in TPM content per gram of soft wet tissue compared to the fresh samples. The processing of clams, like cooking or marinating, caused the content of total soluble extracted proteins to be three to four times lower compared to the other three treatments. In these samples the obtained ratio of the total TPM/ total soluble extracted proteins ratio was the highest. This result can be explained by the fact that TPM is thermostable and stays soluble after cooking, while other proteins become insoluble because of denaturation. The lower ratio of TPM/ total soluble extracted proteins was found in marinated samples compared to the cooked samples. The lowest total tropomyosin/ total soluble extracted proteins ratio was found in 3 days’ shelf-life. Treatments like cooking, marinating and keeping the inner content of the shell at +4°C can significantly affect extractability of proteins, particularly affecting the ratio of major allergen TPM in the total protein extracts. Further studies are needed to examine bioaccessibility of TPM in different biologically relevant fluids (gastric/intestinal) and during digestion in relation to the processing conditions.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "XXII EuroFoodChem conference, Book of Abstracts, 14th-16th June, 2023.",
title = "The effect of food processing and packaging of clams on the content of tropomyosin",
pages = "240-240",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6023"
}