Hvilken av øvelsene nedtrekk, pullups og sittende roing aktiverer m. latissimus dorsi i størst grad?

Sammendrag Vi ønsket å finne ut i hvor stor grad nedtrekk, pullups og sittende roing aktiverte m. latissimus dorsi med overflate elektromyografi (EMG). Nedtrekk er en øvelse som er hyppig brukt blant utøvere og mosjonister som vil bygge nok styrke til å klare sin første pullup med egen kroppsvekt. Pullups er en styrkeøvelse som også er ofte brukt, men dette er en øvelse som stiller store krav til styrke i overkroppen. Sittende roing med smalt nøytralt grep er en øvelse som også blir sett på som en svært god øvelse for m. latissimus dorsi. Muskelaktiviteten ble målt med en elektromyografi-måler med tilhørende overflateelektroder som ble plassert på m. latissimus dorsi på forsøkspersonens høyre side. Resultatene viser at det ikke er noen signifikante forskjeller mellom øvelsene, hverken i gjennomsnittlig aktivering eller maksimal aktivering. Pullups ga en gjennomsnittlig aktivering på 56,4 %, sittende roing 46,8 % og nedtrekk en aktivering på 43,7 %. Pullups har den høyeste maksimalaktiveringen med 141,1 %, nedtrekk den nest høyeste med 121,0 % og sittende roing den laveste maksimalaktiveringen med 106,7 %

Genome-wide analysis of signal peptide functionality in Lactobacillus plantarum WCFS1

<p>Abstract</p> <p>Background</p> <p><it>Lactobacillus plantarum </it>is a normal, potentially probiotic, inhabitant of the human gastrointestinal (GI) tract. The bacterium has great potential as food-grade cell factory and for <it>in situ </it>delivery of biomolecules. Since protein secretion is important both for probiotic activity and in biotechnological applications, we have carried out a genome-wide experimental study of signal peptide (SP) functionality.</p> <p>Results</p> <p>We have constructed a library of 76 Sec-type signal peptides from <it>L. plantarum </it>WCFS1 that were predicted to be cleaved by signal peptidase I. SP functionality was studied using staphylococcal nuclease (NucA) as a reporter protein. 82% of the SPs gave significant extracellular NucA activity. Levels of secreted NucA varied by a dramatic 1800-fold and this variation was shown not to be the result of different mRNA levels. For the best-performing SPs all produced NucA was detected in the culture supernatant, but the secretion efficiency decreased for the less well performing SPs. Sequence analyses of the SPs and their cognate proteins revealed four properties that correlated positively with SP performance for NucA: high hydrophobicity, the presence of a transmembrane helix predicted by TMHMM, the absence of an anchoring motif in the cognate protein, and the length of the H+C domain. Analysis of a subset of SPs with a lactobacillal amylase (AmyA) showed large variation in production levels and secretion efficiencies. Importantly, there was no correlation between SP performance with NucA and the performance with AmyA.</p> <p>Conclusion</p> <p>This is the first comprehensive experimental study showing that predicted SPs in the <it>L. plantarum </it>genome actually are capable of driving protein secretion. The results reveal considerable variation between the SPs that is at least in part dependent on the protein that is secreted. Several SPs stand out as promising candidates for efficient secretion of heterologous proteins in <it>L. plantarum</it>. The results for NucA provide some hints as to the sequence-based prediction of SP functionality, but the general conclusion is that such prediction is difficult. The vector library generated in this study is based on exchangeable cassettes and provides a powerful tool for rapid experimental screening of SPs.</p

Biochemical and structural characterisation of a family GH5 cellulase from endosymbiont of shipworm P. megotara

Background Cellulases play a key role in the enzymatic conversion of plant cell-wall polysaccharides into simple and economically relevant sugars. Thus, the discovery of novel cellulases from exotic biological niches is of great interest as they may present properties that are valuable in the biorefning of lignocellulosic biomass. Results We have characterized a glycoside hydrolase 5 (GH5) domain of a bi-catalytic GH5-GH6 multi-domain enzyme from the unusual gill endosymbiont Teredinibacter waterburyi of the wood-digesting shipworm Psiloteredo megotara. The catalytic GH5 domain, was cloned and recombinantly produced with or without a C-terminal family 10 carbohydrate-binding module (CBM). Both variants showed hydrolytic endo-activity on soluble substrates such as β-glucan, carboxymethylcellulose and konjac glucomannan, respectively. However, low activity was observed towards the crystalline form of cellulose. Interestingly, when co-incubated with a cellulose-active LPMO, a clear syn‑ ergy was observed that boosted the overall hydrolysis of crystalline cellulose. The crystal structure of the GH5 catalytic domain was solved to 1.0 Å resolution and revealed a substrate binding cleft extension containing a putative+3 subsite, which is uncommon in this enzyme family. The enzyme was active in a wide range of pH, temperatures and showed high tolerance for NaCl. Conclusions This study provides significant knowledge in the discovery of new enzymes from shipworm gill endo‑ symbionts and sheds new light on biochemical and structural characterization of cellulolytic cellulase. Study demon‑ strated a boost in the hydrolytic activity of cellulase on crystalline cellulose when co-incubated with cellulose-active LPMO. These findings will be relevant for the development of future enzyme cocktails that may be useful for the biotechnological conversion of lignocellulose

Discovery, characterization and engineering of bacterial thermostable cellulose- degrading enzymes

Lignocellulose is the most abundant biomass on Earth, and thus our largest organic carbon reservoir. Enzymatic depolymerization of recalcitrant polysaccharides, notably cellulose, is a major cost driver in accessing the renewable energy stored within lignocellulosic biomass. Natural biodiversities may be explored to discover microbial enzymes that have evolved to conquer this task in various environments. We are studying novel enzymes from various biodiversities for the conversion of lignocellulosic materials, using (meta)genome mining and functional screening of fosmid libraries. Targeted biodiversities include deep-sea hot vents of the Arctic mid-ocean ridge (AMOR), the microbiome of the wood-eating Arctic shipworm, thermophilic enrichment cultures from biogas reactors, the Svalbard reindeer gut microbiome, and publicly available metagenomic data from various hot environments. Bioprospecting of the different biodiversities has so far resulted in the discovery of approximately 20 novel enzymes active on lignocellulosic substrates. The significant differences in the origin of the enzymes is reflected in their properties, both beneficial and challenging, and provide us with interesting engineering targets for improved performance in industrial settings. We will present case studies, including work on a novel thermostable cellulase named mgCel6A, with good activity on sulfite-pulped Norway spruce. This enzyme consists of a glycoside hydrolase family 6 catalytic domain (GH6) connected to a family 2 carbohydrate binding module (CBM2) and both the activity profile and predicted structural similarities to known cellulases suggest that mgCel6A is an endo-acting cellulase. Comparison of the full-length enzyme with the catalytic domain showed that the CBM strongly increases substrate binding, while not affecting thermal stability. However, importantly, in reactions with higher substrate concentrations the full-length enzyme was outperformed by the catalytic domain alone, underpinning previous suggestions that CBMs may be less useful in high-consistency bioprocessing. This enzyme is currently being targeted for rational engineering in an effort to decrease the pH optimum and improve the pH stability. Other case studies include GH48 cellulases and lytic polysaccharide monooxygenases (LPMOs). One important aspect of this work concerns the possible assembly of novel enzyme cocktails for lignocellulose processing that can compete with exiting commercial cocktails, which are primarily composed of fungal enzymes. Thus, comparative studies of our most promising bacterial enzymes with their well-known fungal counterparts are also being conducted

Hvilken av øvelsene nedtrekk, pullups og sittende roing aktiverer m. latissimus dorsi i størst grad?

Sammendrag Vi ønsket å finne ut i hvor stor grad nedtrekk, pullups og sittende roing aktiverte m. latissimus dorsi med overflate elektromyografi (EMG). Nedtrekk er en øvelse som er hyppig brukt blant utøvere og mosjonister som vil bygge nok styrke til å klare sin første pullup med egen kroppsvekt. Pullups er en styrkeøvelse som også er ofte brukt, men dette er en øvelse som stiller store krav til styrke i overkroppen. Sittende roing med smalt nøytralt grep er en øvelse som også blir sett på som en svært god øvelse for m. latissimus dorsi. Muskelaktiviteten ble målt med en elektromyografi-måler med tilhørende overflateelektroder som ble plassert på m. latissimus dorsi på forsøkspersonens høyre side. Resultatene viser at det ikke er noen signifikante forskjeller mellom øvelsene, hverken i gjennomsnittlig aktivering eller maksimal aktivering. Pullups ga en gjennomsnittlig aktivering på 56,4 %, sittende roing 46,8 % og nedtrekk en aktivering på 43,7 %. Pullups har den høyeste maksimalaktiveringen med 141,1 %, nedtrekk den nest høyeste med 121,0 % og sittende roing den laveste maksimalaktiveringen med 106,7 %

Identification and characterization of a hyperthermophilic GH9 cellulase from the Arctic Mid-Ocean Ridge vent field

A novel GH9 cellulase (AMOR_GH9A) was discovered by sequence-based mining of a unique metagenomic dataset collected at the Jan Mayen hydrothermal vent field. AMOR_GH9A comprises a signal peptide, a catalytic domain and a CBM3 cellulose-binding module. AMOR_GH9A is an exceptionally stable enzyme with a temperature optimum around 100°C and an apparent melting temperature of 105°C. The novel cellulase retains 64% of its activity after 4 hours of incubation at 95°C. The closest characterized homolog of AMOR_GH9A is TfCel9A, a processive endocellulase from the model thermophilic bacterium Thermobifida fusca (64.2% sequence identity). Direct comparison of AMOR_GH9A and TfCel9A revealed that AMOR_GH9A possesses higher activity on soluble and amorphous substrates (phosphoric acid swollen cellulose, konjac glucomannan) and has an ability to hydrolyse xylan that is lacking in TfCel9A.publishedVersio

Do pre-hospital anaesthesiologists reliably predict mortality using the NACA severity score? A retrospective cohort study

Introduction: The National Advisory Committee on Aeronautics’ (NACA) severity score is widely used in pre-hospital emergency medicine to grade the severity of illness or trauma in patient groups but is scarcely validated. The aim of this study was to assess the score’s ability to predict mortality and need for advanced in-hospital interventions in a cohort from one anaesthesiologistmanned helicopter service in Northern Norway. Methods: All missions completed by one helicopter service during January 1999 to December 2009 were reviewed. One thousand eight hundred forty-one patients were assessed by the NACA score. Pre-hospital and in-hospital interventions were collected from patient records. The relationship between NACA score and the outcome measures was assessed using receiver operating characteristic (ROC) curves. Results: A total of 1533 patients were included in the analysis; uninjured and dead victims were excluded per protocol. Overall mortality rate of the patients with NACA score 1–6 was 5.2%. Trauma patients with NACA score 1–6 had overall mortality rate of 1.9% (12/625) and non-trauma patients 7.4% (67/908). The NACA score’s ability to predict mortality was assessed by using ROC area under curve (AUC) and was 0.86 for all, 0.82 for non-trauma and 0.98 for trauma patients. The NACA score’s ability to predict a need for respiratory therapy within 24 h revealed an AUC of 0.90 for all patients combined. Conclusion: The NACA score had good discrimination for predicting mortality and need for respiratory therapy. It is thus useful as a tool to measure overall severity of the patient population in this kind of emergency medicine system

Identification and characterization of a hyperthermophilic GH9 cellulase from the Arctic Mid-Ocean Ridge vent field

A novel GH9 cellulase (AMOR_GH9A) was discovered by sequence-based mining of a unique metagenomic dataset collected at the Jan Mayen hydrothermal vent field. AMOR_GH9A comprises a signal peptide, a catalytic domain and a CBM3 cellulose-binding module. AMOR_GH9A is an exceptionally stable enzyme with a temperature optimum around 100°C and an apparent melting temperature of 105°C. The novel cellulase retains 64% of its activity after 4 hours of incubation at 95°C. The closest characterized homolog of AMOR_GH9A is TfCel9A, a processive endocellulase from the model thermophilic bacterium Thermobifida fusca (64.2% sequence identity). Direct comparison of AMOR_GH9A and TfCel9A revealed that AMOR_GH9A possesses higher activity on soluble and amorphous substrates (phosphoric acid swollen cellulose, konjac glucomannan) and has an ability to hydrolyse xylan that is lacking in TfCel9A

Identification and characterization of a hyperthermophilic GH9 cellulase from the Arctic Mid-Ocean Ridge vent field

A novel GH9 cellulase (AMOR_GH9A) was discovered by sequence-based mining of a unique metagenomic dataset collected at the Jan Mayen hydrothermal vent field. AMOR_GH9A comprises a signal peptide, a catalytic domain and a CBM3 cellulose-binding module. AMOR_GH9A is an exceptionally stable enzyme with a temperature optimum around 100°C and an apparent melting temperature of 105°C. The novel cellulase retains 64% of its activity after 4 hours of incubation at 95°C. The closest characterized homolog of AMOR_GH9A is TfCel9A, a processive endocellulase from the model thermophilic bacterium Thermobifida fusca (64.2% sequence identity). Direct comparison of AMOR_GH9A and TfCel9A revealed that AMOR_GH9A possesses higher activity on soluble and amorphous substrates (phosphoric acid swollen cellulose, konjac glucomannan) and has an ability to hydrolyse xylan that is lacking in TfCel9A

Cell Wall Anchoring of the 37-Kilodalton Oncofetal Antigen by Lactobacillus plantarum for Mucosal Cancer Vaccine Delivery ▿

The 37-kDa oncofetal antigen (OFA), a tumor immunogen expressed on all mammalian cancers examined to date, was secreted and anchored to the cell wall of Lactobacillus plantarum using homologous signal peptides and LPxTG anchors. Orally administered L. plantarum expressing anchored OFA induced a specific immune response against OFA in mice