<i>In Vivo</i> Enzyme Entrapment in a Protein Crystal
Bradley S. Heater, Zaofeng Yang, Marianne M. Lee, Michael K. Chan
Abstract
lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications.
Topics & Concepts
ChemistryThermostabilityLipaseProtein crystallizationBiocatalysisBacillus thuringiensisEnzymeNanoporousEntrapmentImmobilized enzymeBiochemistryBacteriaCatalysisCrystallizationOrganic chemistryBiologyMedicineSurgeryGeneticsIonic liquidEnzyme Catalysis and ImmobilizationMass Spectrometry Techniques and ApplicationsProtein purification and stability