Joana da Costa Ores

A Review of the Latest Advances in Encrypted Bioactive Peptides from Protein-Rich Waste

Bioactive peptides are considered the new generation of biologically active regulators that not only prevent the mechanism of oxidation and microbial degradation in foods but also enhanced the treatment of various diseases and disorders, thus increasing quality of life. This review article emphasizes recent advances in bioactive peptide technology, such as: (i) new strategies for transforming bioactive peptides from residual waste into added-value products; (ii) nanotechnology for the encapsulation, protection and release of controlled peptides; and (iii) use of techniques of large-scale recovery and purification of peptides aiming at future applications to pharmaceutical and food industries.

Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide

This work presents a study of industrially applicable techniques to obtain a biologically supported carbon dioxide capture system, based on the extraction of carbonic anhydrase from bovine blood. Carbonic anhydrase is a metalloenzyme which catalyzes the reversible hydration of carbon dioxide. The objective of this study was to establish conditions to obtain carbonic anhydrase from bovine erythrocytes and apply it in the capture of carbon dioxide. To achieve this, two different purification techniques were evaluated: one by extraction with the organic solvents chloroform and ethanol, where different solvent proportions were studied; and the other by ammonium sulfate precipitation, testing percent saturations between 10% and 80%. Carbon dioxide was enzymatically captured by its precipitation as calcium carbonate with the enzyme obtained by both techniques. The enzyme extracted by ethanol and chloroform showed an activity of 2623 U mL(-1), recovery of 98% and purification factor of 104-fold. That precipitated by ammonium sulfate showed an activity of 2162 U mL(-1), recovery of 66% and purification factor of 1.4-fold using 60% ammonium sulfate saturation. The results obtained in the carbon dioxide capture experiments showed that the carbonic anhydrase extracted in this study not only enhanced the hydration of CO(2), but also promoted the formation of CaCO(3).

Co-production of carbonic anhydrase and phycobiliproteins by Spirulina sp. and Synechococcus nidulans

The aim of this work was to study the co-production of the carbonic anhydrase, C-phycocyanin and allophycocyanin during cyanobacteria growth. Spirulina sp. LEB 18 demonstrated a high potential for simultaneously obtaining the three products, achieving a carbonic anhydrase (CA) productivity of 0.97U/L/d and the highest C-phycocyanin (PC, 5.9μg/mL/d) and allophycocyanin (APC, 4.3μg/mL/d) productivities. In the extraction study, high extraction yields were obtained from Spirulina using an ultrasonic homogenizer (CA: 25.5U/g; PC: 90mg/g; APC: 70mg/g). From the same biomass, it was possible to obtain three biomolecules that present high industrial value.

One-Step Ultrafiltration Process for Separation and Purification of a Keratinolytic Protease Produced with Feather Meal

A purification technique to obtain keratinolytic proteases produced by Bacillus sp. P45 in a medium containing chicken feather meal as substrate is presented. The experiments were carried out in a dead-end ultrafiltration unit, and the influence of the membrane cutoff, pH of enzymatic extract, and operating pressure on the purification of keratinase were studied. The one-step ultrafiltration process with the membrane molecular mass cutoff of 10 kDa at pH 8.0 and operating pressure of 0.147 MPa showed an enzyme recovery of 87.8% and a 4.1-fold purification factor. It is showed that ultrafiltration could be potentially used in the purification of keratinases.