TY - BOOK

T1 - Dynamic Properties of Savinase by Integrative Structural Biology — Indications to Structural Stability

AU - Wu, Shanshan

PY - 2017

Y1 - 2017

N2 - In recent years, enzymes have become widely used as the additives in laundry products forreducing the energy consumption and satisfying the customer-expected cleaning effect.Boosting the stability of these enzymes has become a crucial task in both industry andlaboratory. Subtilisin savinase, as an enzyme product from Novozymes A/S, has these typesof needs as well, since it is usually subjected to the auto-proteolysis issues in the aqueoussolution.The overall purpose of this project is to integratively characterize the structural properties andconformational dynamics in savinase by multiple experimental techniques. The results fromthese studies can indicate the structural stability of savinase. In addition, the work in thisthesis will deposit several structural datasets that are derived from a variety ofcharacterization techniques (including x-ray crystallography, hydrogen-deuterium exchangeby mass spectrometry and solution nuclear magnetic resonance spectroscopy), thereforeoffering a rich source of structural information for the future rational design of savinase.The thesis begins with the background knowledge of enzyme stability. In the subsequentchapter, the background of the targeted enzyme for these structural studies, savinase, isintroduced. Chapter 3 briefly introduces the experimental techniques for studying thestructural insights and conformational fluctuations of savinase, including x-raycrystallography, hydrogen-deuterium exchange mass spectrometry (HDX-MS), and solutionnuclear magnetic resonance (NMR) spectroscopy. In the following chapter of the results, Idescribed all the results of x-ray crystallographic, HDX-MS, and solution NMR studies. Inthe end, the conclusions and the future perspectives are addressed, majorly focus on thestructural stability of savinase. Several relevant appendices are attached with this thesis.

AB - In recent years, enzymes have become widely used as the additives in laundry products forreducing the energy consumption and satisfying the customer-expected cleaning effect.Boosting the stability of these enzymes has become a crucial task in both industry andlaboratory. Subtilisin savinase, as an enzyme product from Novozymes A/S, has these typesof needs as well, since it is usually subjected to the auto-proteolysis issues in the aqueoussolution.The overall purpose of this project is to integratively characterize the structural properties andconformational dynamics in savinase by multiple experimental techniques. The results fromthese studies can indicate the structural stability of savinase. In addition, the work in thisthesis will deposit several structural datasets that are derived from a variety ofcharacterization techniques (including x-ray crystallography, hydrogen-deuterium exchangeby mass spectrometry and solution nuclear magnetic resonance spectroscopy), thereforeoffering a rich source of structural information for the future rational design of savinase.The thesis begins with the background knowledge of enzyme stability. In the subsequentchapter, the background of the targeted enzyme for these structural studies, savinase, isintroduced. Chapter 3 briefly introduces the experimental techniques for studying thestructural insights and conformational fluctuations of savinase, including x-raycrystallography, hydrogen-deuterium exchange mass spectrometry (HDX-MS), and solutionnuclear magnetic resonance (NMR) spectroscopy. In the following chapter of the results, Idescribed all the results of x-ray crystallographic, HDX-MS, and solution NMR studies. Inthe end, the conclusions and the future perspectives are addressed, majorly focus on thestructural stability of savinase. Several relevant appendices are attached with this thesis.

UR - https://soeg.kb.dk/permalink/45KBDK_KGL/fbp0ps/alma99122540396805763

M3 - Ph.D. thesis

BT - Dynamic Properties of Savinase by Integrative Structural Biology — Indications to Structural Stability

PB - Department of Biology, Faculty of Science, University of Copenhagen

ER -