What are the impacts associated with the replacement of sodium alginate with corn starch on bead formation by jet cutting? The case of Eversa Transform 2.0 immobilization

• Published in: Process biochemistry (1991) 2024-08, Vol.143, p.117-127
• Main Authors: Almeida, Francisco Lucas Chaves, Silveira, Mariana Pereira, dos Passos, Rafaela Menezes, da Silva, Thiago Lopes, Sampaio, Klicia Araujo, Vieira, Melissa Gurgel Adeodato, Prata, Ana Silvia, Forte, Marcus Bruno Soares
• Format: Article
• Language: English
• Subjects: Biofuels; Lipase entrapment; Thermal stability
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2024.04.028

Entrapment is a strategy widely used for lipase immobilization and recovery. However, mass transfer issues and the high costs of bead production limit the potential of the technique. This study aimed to investigate the impacts associated with the replacement of sodium alginate with corn starch on bead formation by jet cutting. BET analysis showed surface areas of 1.02 and 1.24 m2 g−1 for beads containing 25 % (B25) and 50 % (B50) starch, respectively. XPS showed nitrogen distribution rates of 7.40–8.77 % (B25) and 4.75–5.10 % (B50). Both immobilized derivatives achieved activity recoveries of 56.23 % ± 5.73 % (B25) and 51.58 % ± 5.56 % (B50) and maximum specific activity of 1500 U g−1 protein. The thermal inactivation constant values of free lipase were 0.0096 and 0.0285 min−1 at 70 and 75 °C, while to immobilized lipases were 7-fold and 2-fold lower than that at 70 and 75 °C, respectively. The half-life time of free lipase and immobilized derivatives (B25 and B50), at 70º C, were 72.20, 577.62 and 533.19 min, respectively. Biodiesel yields of 50.49 % ± 5.67 % and 51.16 % ± 9.91 % were achieved using B25 and B50, respectively. These findings demonstrate lipase can be successfully immobilized on alginate–starch beads by jet cutting. [Display omitted] •Alginate–starch beads were produced by jet cutting.•Eversa Transform 2.0 was successfully entrapped in alginate–starch beads.•XPS showed a uniform nitrogen distribution in inner and outer layers.•The kd of free lipase was 7.38- and ∼2-fold higher than that of immobilized lipases.•Both immobilized lipases were able to produce biodiesel.