The aim of this study was to investigate the effect of an Olympic-Weightlifting-session followed by 48-h recovery period on the oxidative and antioxidant parameters' diurnal variation. Nine weightlifters (21 ± 0.5 years) performed, in randomized order, three Olympic-Weightlifting-sessions at 08 h:00, 14 h:00 and 18 h:00. Blood samples were collected: at rest and 3 min and 48 h after each session. C-reactive protein (CRP), rate of lipid peroxidation and antioxidant activities were assessed. At rest, analysis of variance showed a significant time of day (TOD) effect (p < 0.05) for uric acid, catalase and glutathione peroxidase with higher values at 14 h:00 and 18 h:00 compared with 08 h:00. However, no significant TOD effect for malondialdehyde, total bilirubin and CRP was observed. Given the profound changes (p < 0.001) in the post-training session values, these diurnal variations have been altered immediately and even 48 h after the training sessions. Despite the significant decreases in the post-training values after the 48-h recovery period (p < 0.05), levels of lipid peroxidation and enzymatic defense remained elevated (p < 0.05) 48 h after the morning training session. However, after the afternoon and evening sessions, the same period was sufficient to return values to the baseline levels. In conclusion, the morning session seems to generate the most important acute and delayed lipid peroxidation responses. Therefore, weightlifting coaches should avoid scheduling their training sessions in the morning-hours.

AmyUS100DeltaIG is a variant of the most thermoactive and thermostable maltohexaose forming alpha-amylase produced by Geobacillus stearothermophilus sp.US100. This enzyme which was designed to improve the thermostability of the wild-type enzyme has acquired a very high resistance to chelator agents. According to modeling structural studies and with the aim of enhancing its resistance towards chemical oxidation, a mutant (AmyUS100DeltaIG/M197A) was created by substituting methionine 197 to alanine. The catalytic proprieties of the resulting mutant show alterations in the specific activity and the profile of starch hydrolysis. Interestingly, AmyUS100DeltaIG/M197A displayed the highest resistance to oxidation compared to the AmyUS100DeltaIG and to Termamyl300, the well-known commercial amylase used in detergent. Further, performance of the engineered alpha-amylase was estimated in the presence of commonly used detergent compounds and a wide range of commercial detergent (liquid and solid). These studies indicated a high compatibility and performance of AmyUS100DeltaIG/M197A, suggesting its potential application in detergent industry.

^Äëíê~Åí= The newly Tunisian soil-isolated bacterium, producing the alkaline proteinase termed SAPB that was already purified and characterized [1], was assigned as _~Åáääìë=éìãáäìë=CBS strain on the basis of biochemical properties and 16S rRNA gene sequencing. The maximum protease activity recorded after 24 h of incubation in an optimized medium at 37°C was 6,500 U/mL in shaking flask culture and 25,000 U/mL in fermentor. SAPB showed excellent stability and compatibility in laundry detergent retaining more than 98% of its initial activity after pre-incubation for 1 h at 40°C with Det, followed by OMO (97%), Dinol (94%), and Dixan (93%). Examination of various stained cloth pieces exhibited a remarkable efficiency in the removal of blood and chocolate stains. More interestingly, SAPB demonstrated powerful dehairing capabilities of hair removal from skin with minimal damage on the collagen and a nearly complete feather-degradation. Likewise, _~Åáääìë=éìãáäìë CBS effectively degraded feather-meal (98.5%), chicken feather (92%), goat hair (80%), and bovine hair (68%) whereas sheep wool under went less degradation. Keratin-degradation resulted in sulfhdryl group formation (0.95~3.91 µM). © KSBB hÉóïçêÇëW=^äâ~äáåÉ=éêçíÉáå~ëÉI=Bacillus pumilus=`_pI=ä~ìåÇêó=ÇÉíÉêÖÉåíI=ÇÉÜ~áêáåÖ=ÑìåÅíáçåI=âÉê~íáåJÇÉÖê~Ç~íáçå

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The implications of Asn315 and Val450 in the atypical starch hydrolysis profile of Bacillus stearothermophilus Amy (a-amylase) US100 have been suggested previously [Ben Ali, Mhiri, Mezghani and Bejar (2001) Enzyme Microb. Tech. 28, 537-542]. In order to confirm this hypothesis, three mutants were generated. Of these two have a single mutation, N315D or V450G, whereas the third contains both mutations. Analysis of the starch breakdown-profile of these three mutants, as well as of the wild-type, allowed us to conclude that each single mutation induces a small variation in the hydrolysis product. However, the major end product produced by the double mutant shifts from maltopentaose/maltohexaose to maltose/maltotriose, confirming the involvement of these two residues in starch hydrolysis. The superimposition of AmyUS100 model with that of Bacillus licheniformis shows in AmyUS100 an additional loop containing residues Ile214 and Gly215. Remarkably, the deletion of these two residues increases the half-life at 100 degrees C from 15 min to approx. 70 min. Moreover, this engineered amylase requires less calcium, 25 p.p.m. instead of 100 p.p.m., to reach maximal thermostability.

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Newly discovered Erwinia amylovora phages PEar1, PEar2, PEar4 and PEar6 were isolated from three different orchards in North Tunisia to study their potential as biocontrol agents. Illumina sequencing revealed that the PEar viruses carry a single-strand DNA genome between 6608 and 6801 nucleotides and belong to the Inoviridae, making them the first described filamentous phages of E. amylovora. Interestingly, phage-infected cells show a decreased swimming and swarming motility and a cocktail of the four phages can significantly reduce infection of E. amylovora in a pear bioassay, potentially making them suitable candidates for phage biocontrol.