Evaluation of Malolactic Bacteria Associated with Wines from Albariño Variety as Potential Starters: Screening for Quality and Safety.

The biodiversity of lactic acid bacteria in musts and wines of Albariño variety has been studied. The identification of species was addressed through a combination of biochemical and genetic methods (API 50 CHL test, 16S rDNA and gene sequences, Amplified Ribosomal DNA Restriction Analysis -ARDRA- and 16S-26S intergenic region analysis). The results grouped the isolates into six species predominating those of the genus and showing a typical biogeographical distribution.

Optimizing the expression of a Heterologous chitinase: A study of different promoters.

Many relevant applications have been demonstrated for chitinolytic enzymes. However, their successful exploitation depends upon the availability of strains and expression conditions that allow the production of active forms and large quantities of these enzymes. Escherichia coli has been commonly used to express and overproduce different proteins, among them chitinases.

Optimized expression conditions for enhancing production of two recombinant chitinolytic enzymes from different prokaryote domains.

Enhancing functional gene expression is key to high-level production of active chitinases. For this purpose, the effects of culture cell density, inducer concentration, post-induction time and induction temperatures on the functional expression of two different chitinases (HsChiA1p, a family 18 archaeal chitinase and PtChi19p, a family 19 bacterial chitinase) were comparatively investigated. Results showed that the effect of each parameter on the activity of both chitinases was specific to each enzyme.

Albariño wine aroma enhancement through the use of a recombinant polygalacturonase from Kluyveromyces marxianus.

The possible biotechnological application of a recombinant endopolygalacturonase of Kluyveromyces marxianus (KMPG) for the aroma enhancement of Albariño wine was studied. The addition of this enzyme to the must gives rise to a significant increase of the total compounds responsible for the aroma as opposed to the effect when using a commercial pectic enzyme. This increase also results in a significant rise of the odoriferous aglycones which are direct determinants of the aroma.

Functional expression and characterization of a chitinase from the marine archaeon Halobacterium salinarum CECT 395 in Escherichia coli.

The HschiA1 gene of the archaeon Halobacterium salinarum CECT 395 was cloned and overexpressed as an active protein of 66.5 kDa in Escherichia coli. The protein called HsChiA1p has a modular structure consisting of a glycosyl hydrolase family 18 catalytic region, as well as a N-terminal family 5 carbohydrate-binding module and a polycystic kidney domain.