Publications by authors named "Manisha Chownk"

Landfills are repository for complex microbial diversity responsible for bio-degradation of solid waste. To elucidate this complexity, samples from three different landfill sites of North India (sample V: Bhalswa near Karnal byepass road, New Delhi, India; sample T: Chandigarh, India and sample S3: Una, H.P.

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C-Phycocyanin (C-PC) is a natural blue colored protein of . Several methods based on chemical, physical, and enzymatic processes have been reported for the extraction of C-PC. However, most of the processes are either costly and/or time-consuming and/or produce C-PC with less purity.

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Article Synopsis
  • The study investigates transforming rice straw into simple sugars using a process that includes dilute nitric acid pretreatment and enzymatic hydrolysis.
  • Rice straw is separated into pulp and supernatant, which are then hydrolyzed by microbes isolated from soil, yielding glucose.
  • The optimal conditions for nitric acid pretreatment were 30°C at 200 rpm for 72 hours, resulting in the supernatant producing the highest glucose yield of 205 mg/g of rice straw.
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Aim: mbtJ from Mycobacterium tuberculosis H37Rv is a member of mbt A-J operon required for mycobactin biogenesis.

Materials & Methods: The esterase/acetyl-hydrolase activity of mbtJ was determined by pNP-esters/native-PAGE and expression under iron stress by quantitative-PCR. Effect of gene on growth/survival of Mycobacterium was studied using antisense.

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Most of the chemical and biochemical processes used for the de-polymerization of structural polymers of lignocellulosic biomass are environment unfriendly and costly. Here an efficient process based on xylanase, produced by Acinetobacter pittii MASK25 (MTCC 25132), hydrolysis of only physically treated rice straw and corn cob has been developed for the production of xylooligosaccharides. Bacterial strain isolated from soil was found to produce maximum xylanase at 30°C and pH 7.

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Aim: mesT of Mycobacterium tuberculosis, a hypothetical/putative epoxide hydrolase, is predicted to convert toxic epoxides to the more water-soluble and less toxic diols. Detailed characterization of the protein was carried out.

Results: mesT demonstrated esterase as well as epoxide hydrolase activity.

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