Robust nano-enzyme conjugates for the sustainable synthesis of a rare sugar D-tagatose.

Aim of present study was to develop biological catalysts of L-arabinose isomerase (L-AI) by immobilizing on four different supports such as multiwalled carbon nanotube (MWCNT), graphene oxide (GOx), Santa Barbara Amorphous (SBA-15) and mobile composite matter (MCM-41). Also, comparative analysis of the developed catalysts was performed to evolve the best in terms of transformation efficiency for D-tagatose production. The developed nano-enzyme conjugates (NECs) were characterized using the high resolution transmission electron microscopy (HR-TEM) and elemental analysis was performed by energy dispersive X-ray spectroscopy (EDS).

Dual-Enzyme Metal Hybrid Crystal for Direct Transformation of Whey Lactose into a High-Value Rare Sugar D-Tagatose: Synthesis, Characterization, and a Sustainable Process.

A dual-enzyme metal-organic hybrid crystal was constructed through self-assembling of manganese phosphate embedded with β-galactosidase and L-arabinose isomerase for facile synthesis of rare sugar D-tagatose. The synthesized crystal-like hierarchical system (MnHC@β-Gal+L-AI) was extensively characterized for structural features and catalytic reactions. The results indicated that upon immobilization onto the hybrid crystal, the activity of β-galactosidase and L-arabinose iomerase was enhanced by a factor of 1.

Recovery of nanosized silica and lignin from sugarcane bagasse waste and their engineering in fabrication of composite membrane for water purification.

Environmental benign catalytic process was developed for the valorisation of sugarcane bagasse into functional nanomaterials. Bagasse saccharification was carried out with an acid catalyst (HSO 0.5%, wt/wt) to separate sugars after pre-treatment of biomass with ethanol.

Waste valorization: Identification of an ethanol tolerant bacterium Acetobacter pasteurianus SKYAA25 for acetic acid production from apple pomace.

In present study, a potential bacterial isolate Acetobacter pasteurianus SKYAA25 was found to be very effective in the bioconversion of apple pomace to acetic acid. The isolated strain was tolerant to high ethanol concentrations of upto 14% and temperature of 42 °C. Fermentation of apple pomace alone in presence of brewing yeast produced 7.

Isolation and polyphasic characterization of a novel hyper catalase producing thermophilic bacterium for the degradation of hydrogen peroxide.

A newly isolated microbial strain of thermophilic genus Geobacillus has been described with emphasis on polyphasic characterization and its application for degradation of hydrogen peroxide. The validation of this thermophilic strain of genus Geobacillus designated as BSS-7 has been demonstrated by polyphasic taxonomy approaches through its morphological, biochemical, fatty acid methyl ester profile and 16S rDNA sequencing. This thermophilic species of Geobacillus exhibited growth at broad pH and temperature ranges coupled with production of extraordinarily high quantities of intracellular catalase, the latter of which as yet not been reported in any member of this genus.

Tailoring nutritional and process variables for hyperproduction of catalase from a novel isolated bacterium Geobacillus sp. BSS-7.

Background: Catalase (EC 1.11.1.

Recent insights into microbial catalases: isolation, production and purification.

Catalase, an oxidoreductase enzyme, works as a detoxification system inside living cells against reactive oxygen species formed as a by-product of different metabolic reactions. The enzyme is found in a wide range of aerobic and anaerobic organisms. Catalase has also been employed in various analytical and diagnostic methods in the form of biosensors and biomarkers in addition to its other applications in textile, paper, food and pharmaceutical industries.