Naslov
Power of uncharacterized Lactobacillus amylovorus DSM 20531T amylase(s)

Autori
Polenus, Antonela, Slavica, Anita

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
European Summit of Industrial Biotechnology 2017 (esib 2017) / Berg, Gabriele et al. - Graz : Acib, 2017, 174-174

Skup
European Summit of Industrial Biotechnology 2017 (esib 2017)

Mjesto i datum
Graz, Austrija, 14.11.2017. - 16.11.2017

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
Lactobacillus amylovorus, amylase, semi-solid substrates

Sažetak
Lactobacillus amylovorus DSM 20531T possesses an exceptional set of activities and, above all, amylolytic and proteolytic activities make this strain relevant for resource-efficient bioprocesses (1). Exemplary model systems, starch and raw starch pastes, were used as semi-solid substrates and altered to usable intermediates and/or final products. Actually, complete hydrolysis of linear and branched chains of the starch and the raw starch was performed by the strain at laboratory scale under mild conditions. A mixture of starch- and raw starch-derived maltooligosaccharides and fermentable saccharides was produced and it may be used in numerous enzymatic and whole-cell catalyzed reactions. Due to an elegant equilibrium between the (maltooligo)saccharides substrate inhibition does not occur. The strain has ability to conduct hydrolysis of polymeric substrates - (raw) starch and also proteins under harsh conditions (unpublished data). Furthermore, L. amylovorus DSM 20531T simultaneously ferments the (raw) starch- derived saccharides and produces almost theoretical amount of lactic acid, a valuable platform chemical, and discrete quantity of bacterial biomass. Therefore, the strain could be used as a single biocatalyst in a highly- efficient sustainable production of lactic acid directly from raw materials without addition of enzymes and/or chemicals. Wild-type L. amylovorus DSM 20531T produces apparently amylolytic enzymes that are sensitive toward extracellular proteolysis. Three forms ot active enzymes were separated by ion-exchange chromatography and also by affinity chromatography. De novo sequencing of peptides, obtained from the separated active amylolytic enzymes, from tandem mass spectrometry data has been attracting our attention. The complete genome of L. amylovorus DSM 20531T and the nucleotide sequence of the amylase(s) and the protease genes have not yet been determined. It is of utmost importance to apply know-how of a research group who will help us with: sequencing genome of the strain, identification of the enzymes-coding genes, finding convenient vector and overexpression of the enzymes-coding genes in a suitable host. We offer a co-development of the genetically engineered L. amylovorus strain capable of producing the inermediates and the platform chemical from raw materials under moderate conditions.

Izvorni jezik
Engleski

Znanstvena područja
Biotehnologija

POVEZANOST RADA