Sodium alginate is one of the most interesting and the most investigated and applied biopolymers due to its advantageous properties. Among them, easy, simple, mild, rapid, non-toxic gelation by divalent cations is the most important. In addition, it is abundant, low-cost, eco-friendly, bio-compatible, bio-adhesive, biodegradable, stable, etc. All those properties were systematically considered within this review. Carotenoids are functional components in the human diet with plenty of health benefits. However, their sensitivity to environmental and process stresses, chemical instability, easy oxidation, low water solubility, and bioavailability limit their food and pharmaceutical applications. Encapsulation may help in overcoming these limitations and within this review, the role of alginate-based encapsulation systems in improving the stability and bioavailability of carotenoids is explored. It may be concluded that all alginate-based systems increase carotenoid stability, but only those of micro- and nano-size, as well as emulsion-based, may improve their low bioaccessibility. In addition, the incorporation of other biopolymers may further improve encapsulation system properties. Furthermore, the main techniques for evaluating the encapsulation are briefly considered. This review critically and profoundly explains the role of alginates in improving the encapsulation process of carotenoids, suggesting the best alternatives for those systems. Moreover, it provides a comprehensive cover of recent advances in this field.

Wastewaters generated by the textile industry often contain significant amounts of harmful (carcinogenic and mutagenic) cationic dyes, whose efficient removal is of crucial importance. This study investigates the laccase immobilization on biochar obtained from sour cherry stones (SCS-B), as a cost effective adsorbent, and evaluates its application for brilliant green (BG) degradation. The successful immobilization of laccase on biochar was achieved via adsorption and confirmed using scanning electron microscopy (SEM), energy dispersive X-ray analysis (EDX) and Fourier transform infrared spectroscopy (FTIR). An immobilization efficiency of 66% was achieved using 0.274 U/mL of laccase at pH 5 and a temperature of 40 °C. The adsorption kinetics of laccase followed a pseudo-second-order model, indicating that chemical adsorption plays a significant role in the immobilization process. The BG degradation by immobilized system was further optimized by evaluating effects of pH, temperature, dye concentration, and contact time. More than 92% of BG (50 mg/L) was removed within 4 h at pH 5 and temperature of 30 °C. These findings suggest that SCS-B can effectively be used as an enzyme carrier and be further utilized for the removal of emerging pollutants, positioning it as a sustainable solution for wastewater treatment.

Enzymatic hydrolysis of food proteins is convenient method to improve their functional properties and physiological activity. Herein, the successful covalent attachment of alcalase on alginate micron and submicron beads using the carbodiimide based chemistry reaction and the subsequent application of the beads for egg white and soy proteins hydrolysis were studied. In addition to the electrostatic extrusion technique (EE) previously used by others, the potential utilization of a novel ultrasonic spray atomization technique without drying (UA) and with drying (UAD) for alginate submicron beads production has been attempted. The immobilization parameters were optimized on microbeads obtained by EE technique (803 ± 23 µm) with respect to enzyme loading and alcalase activity. UA and UAD techniques resulted in much smaller particles (607 ± 103 nm and 394 ± 51 nm in diameter, respectively), enabling even higher enzyme loading of 671.6 ± 4 mg g⁻¹ on the carrier and the highest immobilized alcalase activity of 2716.1 IU g⁻¹ in the standard reaction. The UAD biocatalyst exhibited also better performances in the real food system based on egg white or soy proteins. It has been shown that the immobilized alcalase can be reused in seven successive soy protein hydrolysis cycles with a little decrease in the activity.