AM-112

Collision induced dissociation (CID) and collision induced unfolding (CIU) experiments are important tools for determining the structures of and differences between biomolecular complexes with mass spectrometry. However, quantitative comparison of CID/CIU data acquired on different platforms or even using different regions of the same instrument can be very challenging due to differences in gas identity and pressure, electric fields, and other experimental parameters. In principle, these can be reconciled by a detailed understanding of how ions heat, cool, and dissociate or unfold in time as a function of these parameters. Fundamental information needed to model these processes for different ion types and masses is their heat capacity as a function of the internal (i.e., vibrational) temperature. Here, we use quantum computational theory to predict average heat capacities as a function of temperature for a variety of model biomolecule types from 100 to 3000 K. On a degree-of-freedom basis, these values are remarkably invariant within each biomolecule type and can be used to estimate heat capacities of much larger biomolecular ions. We also explore effects of ion heating, cooling, and internal energy distribution as a function of time using a home-built program (IonSPA). We observe that these internal energy distributions can be nearly Boltzmann for larger ions (greater than a few kDa) through most of the CID/CIU kinetic window after a brief (few-μs) induction period. These results should be useful in reconciling CID/CIU results across different instrument platforms and under different experimental conditions, as well as in designing instrumentation and experiments to control CID/CIU behavior.

Biological and interfacial imprinting both were effective methods to improve the catalytic performance of lipase in organic solvent. Bioimprinting combined with interfacial activation of lipase was investigated for obtaining imprinted lipase with excellent catalytic performance. Enzymatic synthesis of sucrose-6-acetate in organic solvents to test the performance of imprinted lipase immobilized by adsorbing on macroporous resin. Lipase imprinted by substrate analog (oleic acid) then immobilization catalyzed the synthesis of sucrose-6-acetate with a 1.7 times increase in sucrose esterification rate compared to unimprinted immobilized lipase and a selectivity toward sucrose-6-acetate of 91.7 %. The sucrose esterification rate of reaction catalyzed by immobilized lipase was increased to 2.0 times with addition of sorbitol after imprinting by oleic acid. Imprinting by oleic acid and interfacial effect generated by oleic acid with sorbitol both induced zymoprotein secondary structure change that were conducive to enhance catalytic activity and stability of lipase in organic solvent.