Silvia M. Albillos

In this study, the use of spray-drying technology for encapsulating Flavourzyme^® (protease–peptidase complex) was evaluated to overcome the limitations (low encapsulation efficiency and no large-scale production) of other encapsulation processes. To the best of our knowledge, spray drying has not been applied previously for the immobilization of this enzyme. Firstly, bovine serum albumin (BSA), as a model protein, was encapsulated by spray drying in chitosan and tripolyphoshate (TPP) cross-linked-chitosan shell matrices. The results showed that the chitosan–TPP microcapsules provided a high encapsulation efficiency and better protein stability compared to the non-crosslinked chitosan microcapsules. The effect of enzyme concentration and drying temperature were tested during the spray drying of Flavourzyme^®. In this regard, an activity yield of 88.0% and encapsulation efficiency of 78.6% were obtained with a concentration of 0.1% (v/v) and an inlet temperature of 130 °C. Flavourzyme^®-loaded chitosan microcapsules were also characterized in terms of their size and morphology using scanning electron microscopy and laser diffractometry.

This article details a correction to: Albillos SM, Montero O, Calvo S, Solano B, Trejo JM, Cubo E. Can Plasma α-Synuclein Help Us to Differentiate Parkinson’s Disease from Essential Tremor? Tremor and Other Hyperkinetic Movements. 2021; 11(1): 20, pp. 1–8. DOI: https://doi.org/10.5334/tohm.600

Studies have revealed controversial results regarding the diagnostic accuracy of plasma α-synuclein levels in patients with Parkinson’s disease (PD). This study was aimed to analyze the diagnostic accuracy of plasma α-synuclein in PD versus healthy controls and patients with essential tremor (ET). In this cross-sectional study, we included de novo (n = 19) and advanced PD patients [OFF (n = 33), and On (n = 35) states], patients with ET (n = 19), and controls (n = 35). The total plasma α-synuclein levels were determined using an ELISA sandwich method. We performed adjusted multivariate regression analysis to estimate the association of α-synuclein levels with group conditions [controls, ET, and de novo, OFF and ON-PD]. We studied the diagnostic accuracy of plasma α-synuclein using the area under the curve (AUC). The plasma α-synuclein levels were higher in controls compared to PD and ET (p < 0.0001), discriminating de novo PD from controls (AUC = 0.74, 95% CI 0.60–0.89), with a trend towards in advanced PD (OFF state) from ET (AUC = 0.69, 95% CI 0.53–0.84). This is the first study examining and comparing plasma α-synuclein levels in ET vs. PD and controls. Preliminary findings suggest that plasma α-synuclein levels might help to discriminate de novo and advanced PD from controls and ET.

In this work, we identified glucose and glycerol as tacrolimus repressing carbon sources in the important species Streptomyces tsukubaensis. A genome-wide analysis of the transcriptomic response to glucose and glycerol additions was performed using microarray technology. The transcriptional time series obtained allowed us to compare the transcriptomic profiling of S. tsukubaensis growing under tacrolimus producing and non-producing conditions. The analysis revealed important and different metabolic changes after the additions and a lack of transcriptional activation of the fkb cluster. In addition, we detected important differences in the transcriptional response to glucose between S. tsukubaensis and the model species Streptomyces coelicolor. A number of genes encoding key players of morphological and biochemical differentiation were strongly and permanently downregulated by the carbon sources. Finally, we identified several genes showing transcriptional profiles highly correlated to that of the tacrolimus biosynthetic pathway regulator FkbN that might be potential candidates for the improvement of tacrolimus production.

Some types of flavonoid intermediates seemed to be restricted to plants. Naringenin is a typical plant metabolite, that has never been reported to be produced in prokariotes. Naringenin is formed by the action of a chalcone synthase using as starter 4-coumaroyl-CoA, which in dicotyledonous plants derives from phenylalanine by the action of a phenylalanine ammonia lyase. A compound produced by Streptomyces clavuligerus has been identified by LC–MS and NMR as naringenin and coelutes in HPLC with a naringenin standard. Genome mining of S. clavuligerus revealed the presence of a gene for a chalcone synthase (ncs), side by side to a gene encoding a P450 cytochrome (ncyP) and separated from a gene encoding a Pal/Tal ammonia lyase (tal). Deletion of any of these genes results in naringenin non producer mutants. Complementation with the deleted gene restores naringenin production in the transformants. Furthermore, naringenin production increases in cultures supplemented with phenylalanine or tyrosine. This is the first time that naringenin is reported to be produced naturally in a prokariote. Interestingly three non-clustered genes are involved in naringenin production, which is unusual for secondary metabolites. A tentative pathway for naringenin biosynthesis has been proposed.

Coeliac disease (CD) is an immune-mediated enteropathy resulting from exposure to gluten in genetically predisposed individuals. Gluten proteins are partially digested by human proteases generating immunogenic peptides that cause inflammation in patients carryingHLA-DQ2andDQ8genes. Although intestinal dysbiosis has been associated with patients with CD, bacterial metabolism of gluten has not been studied in depth thus far. The aim of this study was to analyse the metabolic activity of intestinal bacteria associated with gluten intake in healthy individuals, CD patients and first-degree relatives of CD patients. Faecal samples belonging to twenty-two untreated CD patients, twenty treated CD patients, sixteen healthy volunteers on normal diet, eleven healthy volunteers on gluten-free diet (GFD), seventy-one relatives of CD patients on normal diet and sixty-nine relatives on GFD were tested for several proteolytic activities, cultivable bacteria involved in gluten metabolism, SCFA and the amount of gluten in faeces. We detected faecal peptidasic activity against the gluten-derived peptide 33-mer. CD patients showed differences in faecal glutenasic activity (FGA), faecal tryptic activity (FTA), SCFA and faecal gluten content with respect to healthy volunteers. Alterations in specific bacterial groups metabolising gluten such asClostridiumorLactobacilluswere reported in CD patients. Relatives showed similar parameters to CD patients (SCFA) and healthy volunteers (FTA and FGA). Our data support the fact that commensal microbial activity is an important factor in the metabolism of gluten proteins and that this activity is altered in CD patients.

Human gut microbiota involved in gluten metabolism are described for the first time.