13-16 August 2018
SMC Centre
Australia/Sydney timezone

The electronic structure of S-layer proteins from Lactobacillus brevis

Not scheduled
15m
SMC Centre

SMC Centre

Poster Biosurfaces, Interfaces and Nanostructures Poster Session - Main Hall Tuesday

Speaker

Dr Anton Stampfl (Australian Nuclear Science and Technology Organisation)

Description

Bacterial S-layers present an interesting composite material to study. S-layers are crystalline outer-sheaths of some bacteria that consist of a number of proteins. Unit cells are essentially two-dimensional with lattice parameters that are in the order of nanometers. This study attempts to detail the electronic structure from one particular bacterium, Lactobacillus brevis. L. brevis is a rod-shaped gram-positive bacterium from the family of lactic acid bacteria, Lactobacillaceae, that are involved in the fermentation process creating CO2 and lactic acid. Clearly the surface of such bacteria must play a huge role in such heterogeneous fermentation processes. The valence electronic structure of the S-layer of L. brevis is determined using synchrotron-based photoelectron spectroscopy and soft x-ray absorption spectroscopy. Spectra are compared to experimental work on amino-acids and S-layers of Bacillus sphaericus. While indeed possible to identify energy levels with those of natural amino-acids, distinct energy shifts are observed which cannot be reconciled using such simple comparisons. Furthermore a strong nitrogen signal observed in both the occupied and unoccupied energy levels suggests that the L. brevis protein is amine-terminated on the S-layer surface. The presence of amine termination suggests decarboxylase activity related to the fermentation process.

Primary authors

Dr Anton Stampfl (Australian Nuclear Science and Technology Organisation) Dr Susan Graham (ANSTO) Richard Clements Dr Nicola Asquith (ANSTO) Dr Wilde Karyn (ANSTO) Prof. Yeukuang Hwu (Academia Sinica)

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