The novel multi cross-linked enzyme aggregates of protease, lipase, and catalase production from the sunflower seeds, characterization and application.

The cross-linked enzyme aggregates (CLEAs) have numerous economic advantages in the industrial bio catalysis. In the present study, the multi CLEAs containing protease, catalase, and lipase from the sunflower seeds using starch as a cofeeder as well as bovine serum albumin (BSA) are designed and prepared successfully. After optimization, multi CLEAs of enzyme have been prepared with ammonium sulfate (55% w/v), glutaraldehyde (100 mM), and 8 mg/mL of starch or 20 mg/mL of BSA. The activity recovery of protease, catalase, and lipase multi CLEAs-starch are 87, 61, and 60%, respectively. Whereas, CLEAs prepared with BSA are 74, 61, and 50% activity and multi CLEAs only 60, 44, and 41% of protease, catalase, and lipase, respectively. The multi CLEAs were used to catalyze the reactions for enhanced washing process. After adding multi CLEAs-starch, the stain removal percentage of detergents is enhanced by 83%.The present study reports a high stability, simplicity, low cost, and recyclability of the novel multi CLEAs from the sunflower seeds that make them efficient as a highly active biocatalysts in the biotechnological applications. We believe that these novel multi CLEAs present a new approach to the synthesis of multi enzyme biocatalysts from the cheap and friendly environmental sources.

Lipase-based on starch material as a development matrix with magnetite cross-linked enzyme aggregates and its application.

The Fe3O4 magnetic nanoparticles were prepared by precipitating ferrous ion (Fe2+) and ferric ion (Fe3+) in alkaline solution. The Fe3O4 magnetic nanoparticles were modified by tannic acid. After functionalization process, two methods were used to immobilize Lipase on Fe3O4 magnetic nanoparticles. In the first method, novel tannic acid magnetic cross-linked enzyme aggregates of lipase (TA-MNPs-CLEAs) were synthesized by cross-linking of lipase aggregates and starch as co-feeder with Fe3O4 magnetic nanoparticles improved by tannic acid (TA-MNPs). In the second method, the lipase was successfully immobilized on the surface of TA-MNPs. The properties of Fe3O4 and its modified forms were examined by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), vibrating sample magnetometer (VSM), scanning electron microscopy (SEM) and zeta potential measurements. Novel TA-MNPs-lipase and TA-MNPs-CLEAs-starch-lipase were enhanced and provided an effective method to improve the activity and stability of lipase for biodiesel production. Using 1% TA-MNPs-lipase and TA-MNPs-CLEAs-starch (w/w of oil) conversions around 67.87, and 85.88%, respectively, were obtained at 40 °C after 2 h of reaction. Furthermore, the immobilized enzyme was easily recovered from the reaction mixture and reused. The obtained results suggest that TA-MNPs-lipase and TA-MNPs-CLEAs-starch-lipase can become a powerful biocatalyst for biodiesel production.