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Instruments / Technical Area	Publication Details	Published
B21-High Throughput SAXS	Flavour compounds affect protein structure: The effect of methyl anthranilate on bovine serum albumin conformation Vlad Dinu , Pallab Kumar Borah , Molly Muleya , David J Scott , Ryan Lithgo , Jacob Pattem , Stephen E. Harding , Gleb E. Yakubov , Ian D. Fisk Food Chemistry 388 DOI: 10.1016/j.foodchem.2022.133013 Diamond Proposal Number(s): [22113] Show Abstract ▼ Abstract: This study aims to understand possible effects of flavour compounds on the structure and conformation of endogenous proteins. Using methyl anthranilate (a grape flavour compound added to drinks, confectionery, and vape-liquids) and bovine serum albumin (BSA, a model serum protein) we designed experimental investigations using analytical ultracentrifugation, size exclusion chromatography small angle X-ray scattering, and fluorescence spectroscopy to reveal that methyl anthranilate spontaneously binds to BSA (ΔG°, ca. −21 KJ mol−1) which induces a conformational compactness (ca. 10 %) in the monomer structure. Complementary molecular modelling and dynamics simulations suggested the binding occurs at Sudlow II of BSA via establishment of hydrogen bonds with arginine409, lysine413 and serine488 leading to an increased conformational order in domains IA, IIB and IIIB. This work aims to set the foundation for future research on flavour-protein interactions and offer new sets of opportunities for understanding the effects of small compounds on protein structure.	Sep 2022
I03-Macromolecular Crystallography	Crystal structure of levansucrase from the gram-negative bacterium Brenneria provides insights into its product size specificity Wei Xu , Dawei Ni , Xiaodong Hou , Tjaard Pijning , Albert Guskov , Yijian Rao , Wanmeng Mu Journal Of Agricultural And Food Chemistry 30 DOI: 10.1021/acs.jafc.2c01225 Diamond Proposal Number(s): [19800] Show Abstract ▼ Abstract: Microbial levansucrases (LSs, EC 2.4.1.10) have been widely studied for the synthesis of β-(2,6)-fructans (levan) from sucrose. LSs synthesize levan-type fructo-oligosaccharides, high-molecular-mass levan polymer or combinations of both. Here, we report crystal structures of LS from the G–-bacterium Brenneria sp. EniD 312 (Brs-LS) in its apo form, as well as of two mutants (A154S, H327A) targeting positions known to affect LS reaction specificity. In addition, we report a structure of Brs-LS complexed with sucrose, the first crystal structure of a G–-LS with a bound substrate. The overall structure of Brs-LS is similar to that of G–- and G+-LSs, with the nucleophile (D68), transition stabilizer (D225), and a general acid/base (E309) in its active site. The H327A mutant lacks an essential interaction with glucosyl moieties of bound substrates in subsite +1, explaining the observed smaller products synthesized by this mutant. The A154S mutation affects the hydrogen-bond network around the transition stabilizing residue (D225) and the nucleophile (D68), and may affect the affinity of the enzyme for sucrose such that it becomes less effective in transfructosylation. Taken together, this study provides novel insights into the roles of structural elements and residues in the product specificity of LSs.	Apr 2022
B23-Circular Dichroism	Spectroscopy reveals that ethyl esters interact with proteins in wine Mattia Di Gaspero , Paolo Ruzza , Rohanah Hussain , Simone Vincenzi , Barbara Biondi , Diana Gazzola , Giuliano Siligardi , Andrea Curioni Food Chemistry DOI: 10.1016/j.foodchem.2016.08.133 Diamond Proposal Number(s): [11540, 12086] Show Abstract ▼ Abstract: Impairment of wine aroma after vinification is frequently associated to bentonite treatments and this can be the result of protein removal, as recently demonstrated for ethyl esters. To evaluate the existence of an interaction between wine proteins and ethyl esters, the effects induced by these fermentative aroma compounds on the secondary structure and stability of VVTL1, a Thaumatin-like protein purified from wine, was analyzed by Synchrotron Radiation Circular Dichroism (SRCD) spectroscopy. The secondary structure of wine VVTL1 was not strongly affected by the presence of selected ethyl esters. In contrast, VVTL1 stability was slightly increased by the addition of ethyl-octanoate, -decanoate and -dodecanoate, but decreased by ethyl-hexanoate. This indicates the existence of an interaction between VVTL1 and at least some aroma compounds produced during fermentation. The data suggest that proteins removal from wine by bentonite can result in indirect removal of at least some aroma compounds associated with them.	Sep 2016

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