Kashk is a typical dairy product of Iran, made from sour milk. It is traditionally produced from buttermilk in a dry, round-shaped form. Today, it is also produced at industrial level in a liquid form starting from fermented milk. We aimed to characterise the kashk proteome and peptidome comparing a traditional product with the industrial using a combination of proteomic approaches including advanced chromatographic and electrophoretic separation technique coupled to tandem mass spectrometry. We identified also phosphorylated casein-derived peptides (CPP) and investigated kashk protein digestibility using a static model of food protein digestion. The molecular characterization, coupled with bioinformatic in silico analysis, allowed the identification of potential bioactive peptides.
The protein and peptide fractions of kashk, a traditional Middle East fermented dairy product / Pourjoula, Mina; Picariello, Gianluca; Garro, Giuseppina; D'Auria, Giovanni; Nitride, Chiara; Rheza Ghaisari, Amid; Ferranti, Pasquale. - In: FOOD RESEARCH INTERNATIONAL. - ISSN 0963-9969. - (2020). [10.1016/j.foodres.2020.109107]
The protein and peptide fractions of kashk, a traditional Middle East fermented dairy product
Gianluca Picariello;Giuseppina Garro;Giovanni D'Auria;Chiara Nitride;Pasquale Ferranti
2020
Abstract
Kashk is a typical dairy product of Iran, made from sour milk. It is traditionally produced from buttermilk in a dry, round-shaped form. Today, it is also produced at industrial level in a liquid form starting from fermented milk. We aimed to characterise the kashk proteome and peptidome comparing a traditional product with the industrial using a combination of proteomic approaches including advanced chromatographic and electrophoretic separation technique coupled to tandem mass spectrometry. We identified also phosphorylated casein-derived peptides (CPP) and investigated kashk protein digestibility using a static model of food protein digestion. The molecular characterization, coupled with bioinformatic in silico analysis, allowed the identification of potential bioactive peptides.File | Dimensione | Formato | |
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