Application of actinidin as coagulants to produce Iranian white brined cheese: investigating the technological, textural, and sensorial properties (original) (raw)

Journal of Food Measurement and Characterization, 2021

Abstract

In this study, the actinidin was purified by the salt precipitation and anion-exchange chromatography method on the DEAE-Cellulose column. Skim milk powder was used to assay proteolytic activity (PA), and milk clotting activity (MCA) was measured on total casein as substrate. Kiwi juice had less MCA and high PA than Mucor miehei. The kinetic parameters Km and Vmax for actinidin on a casein substrate were 2.72 mM and 1.36 × 10–6 mM/min, respectively. The SDS-PAGE analysis revealed that the molecular weight of the enzyme was 29 KDa and among the casein proteins, β-casein was the main protein that affected by this enzyme. The texture profile of kiwi juice cheese exhibited a softer body and less cohesiveness, gumminess, elasticity and chewiness than cheese made by M. miehei (p < 0.05). Regarding sensorial properties, the texture and taste score of cheese coagulated by fungal protease are significantly higher than cheese produced by kiwifruit protease. However, kiwifruit protease has a lower cost than fungal protease and also has a higher cheese production yield, which is economically important.

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