Properties of cellulases fromSclerotium rolfsii

Summary Filter paper cellulase (FPCase) and carboxymethyl cellulase (CMCase) activities ofSclerotium rolfsii were maximal at pH 4.8 and 3.6, respectively, and at 55°C. Both activities increased three-fold when the concentrations of filter paper and carboxymethylcellulose were increased by six-and five-fold, respectively. Enzyme activities decreased with increasing incubation period though sugar formation increased. The K_m and V_max values activity were 61.5 mg and 0.57 m for FPCase and 6.25 mg and 1.58 m for CMCase.

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Propriétés des celluloses de Sclerotium rolfsii

Résumé Les activités cellulolytiques mesurées sur papier filtre (FPCase) et avec la carboxyméthylcellulose (CMCase) chezSclerotium rolfsii ont leur valeur maximum respectivement à pH 4.8 et 3.6, et à 55°C. Les deux activités augmentent de trois fois quand on augmente les concentrations en papier filtre et en carboxymethylcellulose de six et cinq fois respectivement. Les activités enzymatiques décroissent lorsque la période d'incubation augmente, bien que la formation de sucre croisse. Les valeurs de K_m et V_max sont de 61.5 mg et 0.57 m pour la FPCase et de 6.25 mg et 1.58 m pour la CMCase.

     

Evaluation of chemical pre-treatment for biodegradation of agricultural lignocellulosic wastes byAspergillus niger

Summary Chemical pre-treatment with NaOH, NaClO₂ or peracetic acid of wheat straw, bagasse, corn cobs and groundnut shells increased cellulose utilization, cellulase activity and protein content ofAspergillus niger AS-101 used as a test biodegradative microorganism.

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Resumen El pre-tratamiento químico con NaOH, NaClO2 o àcido peracético de paja de trigo, bagazo, mazorcas de maíz y cáscaras de cacahuete, incrementó la utilización de celulosa, la actividad celulásica y el contenido en proteínas deAspergillus niger AS-101.

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Résumé Le prétraitement chimique par NaOH, NaClO₂ ou par l'acide peracétique de la paille de froment, de la bagasse, des épis de maïs ou des coquilles d'arachide, augmente l'utilisation de la cellulose, l'activité de la cellulase et le contenu en protéines d'Aspergillus niger AS-101, utilisé comme souche test dans la biodégradation par les microorganismes.

     

Retention of plastic-tipped dart tags in African tigerfish Hydrocynus vittatus

Estimates of tag retention and tagging-related mortality are essential for mark-recapture experiments. Mortality and tag loss were estimated from 15 tigerfish Hydrocynus vittatus marked using Hallmark model PDL plastic-tipped dart tags released into a 1 730 m² pond at Kamutjonga Inland Fisheries Institute, Namibia, and inspected bi-monthly for the presence or absence of tags. No mortality was observed during the experiment. All marked fish had lost their tags after 10 months and 50% tag loss was estimated at 3.9 months. The high tag loss rate indicates that PDL plastic-tipped dart tags are not suitable for long-term studies on this species.     

Natural history of SLC11 genes in vertebrates: tales from the fish world

Background  

The SLC11A1/Nramp1 and SLC11A2/Nramp2 genes belong to the SLC11/Nramp family of transmembrane divalent metal transporters, with SLC11A1 being associated with resistance to pathogens and SLC11A2 involved in intestinal iron uptake and transferrin-bound iron transport. Both members of the SLC11 gene family have been clearly identified in tetrapods; however SLC11A1 has never been documented in teleost fish and is believed to have been lost in this lineage during early vertebrate evolution. In the present work we characterized the SLC11 genes in teleosts and evaluated if the roles attributed to mammalian SLC11 genes are assured by other fish specific SLC11 gene members.     

Improved production of alkaline protease from a mutant of alkalophilic Bacillus pantotheneticus using molasses as a substrate

An alkalophilic bacterial isolate identified as Bacillus pantotheneticus, isolated from saline-alkali soils of Avadh region of UP, India, was studied for the production of alkaline protease. The mutant of the isolated species showed 44% improved production over the parent strain. Organic nitrogen sources supported better protease production than the inorganic sources. The production of alkaline protease was (242 U/ml) in the medium containing molasses, which was comparable with molasses and wheat bran (285 U/ml) as carbon and nitrogen sources, respectively. Protease production was best at pH 10 and temperature 30 degrees C. The Km (for casein) was 11 mg/ml and Vmax was 380-microg tyrosine/ml/min. The enzyme was stable between pH 7 and 10.7 and temperature between 30 and 60 degrees C with a pH and temperature optimum at 8.4 and 40 degrees C, respectively. The results indicated that molasses was an optimal substrate for alkaline protease production.     

Properties of cellobiase from Aspergillus niger

Summary Cellobiase enzyme was partially purified from the culture filtrate of Aspergillus niger AS-101 and the general and kinetic properties of the enzyme were examined. The enzyme was unstable on storage. However, it was protected by the addition of BSA, glycerol or sodium azide. Addition of glycerol also protected the enzyme from denaturation due to freezing and thawing. Effect of thiol group reagents revealed the presence of — SH groups at the active site of the enzyme. Different modulators such as metal ions and macroionic compounds illustrated varying effects on the purified cellobiase. Offprint requests to: A. Singh     

Saccharification of cellulosic substrates byAspergillus niger cellulase

Chemical pre-treatment enhanced saccharification of agricultural lignocellulosic residues usingAspergillus niger cellulase by between 16 and 38%. Maximum saccharification (76%) of alkali-treated bagasse was with 0.5% substrate over 48 h using 0.3 U enzyme/ml.

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Résumé Le pré-traitement chimique augmente de 16 à 38% la saccharification de résidus agricoles ligno-cellulosiques lorsque l'on utilise la cellulase d'Aspergillus niger. On a obtenu la saccharification maximum (76%) de la bagasse traitée à l'alcali avec 0.5% de substrat en 48 h de traitement avec 0.3 unités d'enzyme par ml.

     

Xanthomonas campestris, a novel stress tolerant, phosphate-solubilizing bacterial strain from saline–alkali soils

A total of 198 bacterial strains were isolated from various niches of saline–alkali soils, out of which 85 strains were able to solubilize phosphate on plates at 30 °C. The strain RMLU-26, identified as Xanthomonas campestris, was the most efficient with its ability to solubilize P, subjected to N-methyl-N′-nitro-N-nitrosoguanidine (NTG) for development of mutants. The P solubilizing ability of X. campestris is reported for the first time. The wild type and mutant strains of X. campestris revealed a differential response to various stress factors (high pH, temperature, and salt concentration). The mutant strain revealed maximum P solubilization (67.1%) at 30 °C and pH 8.0 while the wild type strain showed maximum solubilization (41.9%) at 35 °C and pH 7.0. Percent P₂O₅ solubilization by both strains revealed a steep decline in tricalcium phosphate solubilization with an increase in NaCl concentration from 0.5 to 10% along with a concomitant drop in pH of the medium from 8.0 to 4.5 in wild type and 4.0 in mutant strain. However, a 1.5- to 2-fold increase in ‘P’ solubilization was observed in the mutant strain when compared to the wild type strain in the presence of NaCl. The overall improved tolerance of the strains to alkalinity and salinity could be due to accumulation and/or secretion of specific solute (xanthan).