Publications by authors named "Adriana Mabel Rosso"

Article Synopsis
  • Recent increases in cheese consumption and the rising cost of traditional rennet have sparked interest in finding plant-based alternatives for cheese production, particularly for those with dietary restrictions.
  • This study investigates an aspartic protease from Salpichroa origanifolia fruits (SoAP), which was found to have lower milk-clotting capabilities compared to animal rennet but showed greater hydrolysis of α-casein.
  • The identification of several bioactive peptides from different casein types suggests that SoAP could not only serve as an alternative rennet but also offer health benefits, making it suitable for artisan cheese manufacturing.
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Chia expeller is a by-product of the extrusion process of chia seeds generated during oil production. Typically, this material is non-utilized or used for non-valuable applications. In the present work, the chia expeller was hydrolysed with Papain and the antioxidant properties of the resultant peptides were evaluated.

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An aspartic protease from Salpichroa origanifolia fruits was successfully immobilized onto an activated support of glutaraldehyde agarose. The immobilized enzyme presented higher thermal stability than the free enzyme from 40°C to 50°C and high reusability, retaining 54% of the initial activity after ten cycles of the process. Whey protein concentrates (WPC) were hydrolyzed with both free and immobilized enzyme, reaching a similar degree of hydrolysis of approximately 6-8% after 20h.

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Cyclodextrins (CD) are cyclic oligosaccharides with multiple applications in the food, pharmaceutical, cosmetic, agricultural and chemical industries. In this work, the conditions used to produce CD with cyclodextrin glycosyltransferase from Bacillus circulans DF 9R were optimized using experimental designs. The developed method allowed the partial purification and concentration of the enzyme from the cultural broth and, subsequently, the CD production, using the same cassava starch as enzyme adsorbent and as substrate.

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