Biotechnology Progress · 2016 · 18 citations · 25 references
EngineeringBioengineeringBiotechnologyBiocatalysisBiochemical EngineeringBiomaterialsBio-based MaterialsBiomaterial CharacterizationPectinases In Food ProcessingImmobilized PectinasesMagnetic NanoparticlesMagnetic Support ImmobilizationNanoparticlesPectate Lyase ActivityPectin Lyase ActivityPectinolytic ActivityThermal Stability
Recombinant pectate lyase from family 1 polysaccharide lyase (PL1B) was immobilized on synthesized magnetic nanoparticles (MNPs) after 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride activation. At 70 mg/mL MNPs 100% binding of 1 mg/mL PL1B was achieved. The immobilized PL1B-MNP displayed activity of 20.3 and 18.2 U/mg against polygalacturonic acid and citrus pectin, respectively, which was higher than the activity of free PL1B, on the same substrates of 17.8 and 16.2 U/mg. The immobilized PL1B-MNP showed 32 fold and 14 fold enhanced thermal stability at 80°C and 90°C, respectively as compared with free PL1B at same temperatures. At high temperature the immobilized PL1B-MNP retained its activity for a longer duration than free PL1B. The immobilized PL1B-MNP could be reused till five cycles and after that it retained 70% of initial activity. It could be easily recovered from the reaction mixture with the help of a magnet. Bioscouring of cotton fabric was carried out with immobilized PL1B-MNP which showed efficient removal of pectin from the fabric surface. The enhanced wettability of fabric resulted in the decrease of the water absorbing time period from 3 min taken by the free PL1B treated fabric to 15 s taken by the immobilized PL1B-MNP treated fabric. As per our knowledge this is the first attempt of bioscouring of coarse cotton fabric by pectinase immobilized on magnetic nanoparticles. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:231-244, 2017.
25
The Scherrer Formula for X-Ray Particle Size Determination
A. L. Patterson · Physical Review · 1939 · 8.9K citations