Anna Rafaela Cavalcante Braga

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.

β-Galactosidase production using glycerol and byproducts: Whey and residual glycerin

Abstract The present study aimed to evaluate β-galactosidase production by liquid-state fermentation using an experimental design and response surface methodology. A culture medium containing lactose and analytical grade glycerol was formulated to maximize β-galactosidase production. The effects of the pH, lactose, and glycerol concentration on the enzyme production were studied using a Central Composite Design (CCD; 23 plus central points), followed by a Central Composite Rotatable Design (CCRD; 23 plus axial and central points). The conditions that maximized β-galactosidase production were: lactose concentration of 20 g L−1, glycerol concentration of 60 g L−1, and pH 5.0. Under these conditions, the highest enzymatic activity was 40.7 U mL−1. Glycerol and lactose were replaced by residual glycerin and whey respectively, according to the best condition obtained in CCRD, reaching enzymatic values of 31.8 U mL−1, and thus demonstrating to be great alternative sources for β-galactosidase production.

Single Chromatographic Step for β-Galactosidase Purification: Influence of Salt and Elution Parameters

β-galactosidase purification was performed by ion exchange chromatography in which the main elution parameters and different elution salts (NaCl, KCl, and (NH4)2SO4) were evaluated through distinct purification strategies. Among the salts under analysis, KCl was the best one for β-galactosidase purification, since it reached a 95.1% recovery and an 8.2-fold purification factor. NaCl, which is the most common elution salt found in the literature, obtained a 75.1% recovery and a 7.5-fold purification factor whereas ammonium sulfate, as salt elution, yielded a 72.1% recovery and a 3-fold purification factor in the same conditions.