Well parameters of two-dimensional electron gas in Al0.88In 0.12N/AlN/GaN/AlN heterostructures grown by MOCVD

Resistivity and Hall effect measurements were carried out as a function of magnetic field (0-1.5 T) and temperature (30-300 K) for Al0.88In 0.12N/AlN/GaN/AlN heterostructures grown by Metal Organic Chemical Vapor Deposition (MOCVD). Magnetic field dependent Hall data were analyzed by using the quantitative mobility spectrum analysis (QMSA). A two-dimensional electron gas (2DEG) channel located at the Al0.88In 0.12N/GaN interface with an AlN interlayer and a two-dimensional hole gas (2DHG) channel located at the GaN/AlN interface were determined for Al 0.88In0.12N/AlN/GaN/AlN heterostructures. The interface parameters, such as quantum well width, the deformation potential constant and correlation length as well as the dominant scattering mechanisms for the Al 0.88In0.12N/GaN interface with an AlN interlayer were determined from scattering analyses based on the exact 2DEG carrier density and mobility obtained with QMSA. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA

Cardiac Alpha-Myosin (MYH6) Is the Predominant Sarcomeric Disease Gene for Familial Atrial Septal Defects

Secundum-type atrial septal defects (ASDII) account for approximately 10% of all congenital heart defects (CHD) and are associated with a familial risk. Mutations in transcription factors represent a genetic source for ASDII. Yet, little is known about the role of mutations in sarcomeric genes in ASDII etiology. To assess the role of sarcomeric genes in patients with inherited ASDII, we analyzed 13 sarcomeric genes (MYH7, MYBPC3, TNNT2, TCAP, TNNI3, MYH6, TPM1, MYL2, CSRP3, ACTC1, MYL3, TNNC1, and TTN kinase region) in 31 patients with familial ASDII using array-based resequencing. Genotyping of family relatives and control subjects as well as structural and homology analyses were used to evaluate the pathogenic impact of novel non-synonymous gene variants. Three novel missense mutations were found in the MYH6 gene encoding alpha-myosin heavy chain (R17H, C539R, and K543R). These mutations co-segregated with CHD in the families and were absent in 370 control alleles. Interestingly, all three MYH6 mutations are located in a highly conserved region of the alpha-myosin motor domain, which is involved in myosin-actin interaction. In addition, the cardiomyopathy related MYH6-A1004S and the MYBPC3-A833T mutations were also found in one and two unrelated subjects with ASDII, respectively. No mutations were found in the 11 other sarcomeric genes analyzed. The study indicates that sarcomeric gene mutations may represent a so far underestimated genetic source for familial recurrence of ASDII. In particular, perturbations in the MYH6 head domain seem to play a major role in the genetic origin of familial ASDII

Unequal allelic expression of wild-type and mutated β-myosin in familial hypertrophic cardiomyopathy

Familial hypertrophic cardiomyopathy (FHC) is an autosomal dominant disease, which in about 30% of the patients is caused by missense mutations in one allele of the β-myosin heavy chain (β-MHC) gene (MYH7). To address potential molecular mechanisms underlying the family-specific prognosis, we determined the relative expression of mutant versus wild-type MYH7-mRNA. We found a hitherto unknown mutation-dependent unequal expression of mutant to wild-type MYH7-mRNA, which is paralleled by similar unequal expression of β-MHC at the protein level. Relative abundance of mutated versus wild-type MYH7-mRNA was determined by a specific restriction digest approach and by real-time PCR (RT-qPCR). Fourteen samples from M. soleus and myocardium of 12 genotyped and clinically well-characterized FHC patients were analyzed. The fraction of mutated MYH7-mRNA in five patients with mutation R723G averaged to 66 and 68% of total MYH7-mRNA in soleus and myocardium, respectively. For mutations I736T, R719W and V606M, fractions of mutated MYH7-mRNA in M. soleus were 39, 57 and 29%, respectively. For all mutations, unequal abundance was similar at the protein level. Importantly, fractions of mutated transcripts were comparable among siblings, in younger relatives and unrelated carriers of the same mutation. Hence, the extent of unequal expression of mutated versus wild-type transcript and protein is characteristic for each mutation, implying cis-acting regulatory mechanisms. Bioinformatics suggest mRNA stability or splicing effectors to be affected by certain mutations. Intriguingly, we observed a correlation between disease expression and fraction of mutated mRNA and protein. This strongly suggests that mutation-specific allelic imbalance represents a new pathogenic factor for FHC

Active Whey Protein Edible Films and Coatings Incorporating Lactobacillus buchneri for Penicillium nordicum Control in Cheese

Fungal contamination of food is responsible for health issues and food waste. In this work, the incorporation of a lactic acid bacteria (LAB) with antifungal properties (Lactobacillus buchneri UTAD104) into whey protein-based films and coatings was tested for the control of an ochratoxigenic fungi (Penicillium nordicum) in a cheese matrix. The incorporation of L. buchneri cells resulted in thicker films with less luminosity than control films and colour alteration. Nevertheless, cells inclusion did not alter moisture content, water vapour permeability, mechanical properties, hydrophobicity and chemical structure of the films. Whey protein films were able to maintain the viability of L. buchneri UTAD104 cells in 105 CFU/mL after 30 days of storage at 25 \textdegreeC. When applied in cheese, films and coatings containing L. buchneri cells prevented fungal contamination for at least 30 days, while control cheeses with films and coatings either without LAB or with Lactobacillus casei UM3 (a strain without antifungal ability) showed fungal contamination during that period. Ochratoxin A was not found in cheeses treated with films and coatings containing L. buchneri UTAD104. Results showed that the inclusion of a LAB with antifungal properties in edible films and coatings can help to reduce or eliminate P. nordicum contamination in cheeses.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UIDB/04469/2020 unit and BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte. Ana Guimarães received support through grant SFRH/BD/103245/2014 from the Portuguese FCT.info:eu-repo/semantics/publishedVersio

Formation of lactic, acetic, succinic, propionic, formic and butyric acid by lactic acid bacteria

Organic acids (lactic, acetic, succinic, propionic, formic and butyric acid) production by lactic acid bacteria (LAB) were investigated in various fish infusion broth (anchovy, sea bass, tilapia and trout) and MRS broth (control) by using HPLC method. Significant differences were found in organic acid levels (P < 0.05) among bacterial strains. Succinic acid formation was the highest by LAB whilst acetic acid was produced at the lowest levels. The highest lactic acid production was observed with Lactobacillus lactis subsp. lactis and Pediococcus acidilactici in anchovy infusion broth, with values of 2403 and 2345 mg/L, respectively. Acetic acid production was 822 and 803 mg/L by Lactobacto acidophilus and Lactobacillus delbrueckii subsp. lactis in anchovy infusion broth, respectively while succinic acid production ranged from 142 mg/L by Lb. delbrueckii subsp. lactis in sea bass infusion broth to 9231 mg/L by Lb. lactis subsp. lactis in MRS broth. Propionic acid formation by Pc. acidilactici was 3747 mg/L in sea bass infusion broth whereas Lb. lactis subsp. cremoris produced less than that in MRS broth. The result of the study indicated that LAB strains had a great ability to produce succinic acid. Also other organic acid production varied significantly depending on bacterial strains and growth medium. © 2016 Elsevier LtdÇukurova Üniversitesi: SÜF2010YL8This study was financially supported by Çukurova University , Scientific Research Projects Coordination Unit (Project No: SÜF2010YL8 )