Bio-nanocomposites for food packaging applications

Trends in bioconversion of lignocellulose: Biofuels, platform chemicals & biorefinery concept

Actinobacteria: Current research and perspectives for bioremediation of pesticides and heavy metals.

The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

/pdf/microbial-proteases-applications-o4nt9ikd6n.pdf

Microbial Proteases Applications.

https://www.cell.com/trends/biotechnology/pdf/S0167-7799(11)00070-9.pdf

Alternatives to Trichoderma reesei in biofuel production.

Optimization and scale up of production of alkaline protease from Conidiobolus coronatus

Studies on biological reduction of chromate by Streptomyces griseus.

The waste X-ray/ photographic films contain 1.5 - 2 % (w/w) black metallic silver which is recovered and reused. Around 18-20% of the world's silver needs are supplied by recycling photographic waste. Since silver is linked to gelatin in the emulsion layer, it is possible to break the same and release the silver using proteolytic enzymes. Alkaline protease from Conidiobolus coronatus was investigated for enzymatic hydrolysis of gelatin from waste X-ray films. At the end of the treatment, gelatin layer was completely removed leaving the polyester film clean and silver was recovered in the hydrolysate, both of which can be reused. Various parameters such as pH, temperature, enzyme concentration, time etc on silver removal from the film were studied. Gelatin hydrolysis was monitored by measuring increase in turbidity in the hydrolysate, which was accompanied by release of protein and hydroxyproline. Gelatin layer was stripped completely within 6 min with 1.35 U ml -1 of protease at 40°C, pH 10. Rate of gelatin hydrolysis increased with increased in protease concentration. The enzyme could be effectively reused for four cycles of gelatin hydrolysis. Silver in hydolysate was around 3.87% (w/w) based on total weight of sludge. Key words: Silver recovery; X-ray films; gelatin hydrolysis; alkaline protease; Conidiobolus coronatus DOI: 10.3126/kuset.v6i1.3311 Kathmandu University Journal of Science, Engineering and Technology Vol.6(1) 2010, pp60-69

/pdf/recovery-of-silver-from-waste-x-ray-film-by-alkaline-3rrqneabzg.pdf

Recovery of Silver from Waste X-Ray Film by Alkaline Protease from Conidiobolus coronatus

An effective alkali pretreatment which affects the structural properties of cellulose (corn cob) has been studied. The pretreatment of corn cob was carried out with different combinations of alkali at varying temperatures. The most effective pretreatment of corn cob was achieved with 1 % alkali at 50 °C in 4 h. The crystallinity index (CrI) and specific surface area (SSA) of untreated corn cob was 39 % and 0.52 m2/g wherein after alkali pretreatment CrI decreased to 15 % and SSA increased to 3.32 m2/g. The fungal organism was identified as Penicillium pinophilum on the basis of ITS sequence. At 5 % substrate concentration using a complete cellulase from Penicillium pinophilum the hydrolysis of untreated corn cob with 5, 10 and 20 FPU/g enzyme loadings were 11 %, 13 % and 16 %, whereas after alkali treatment the hydrolysis increased to 78 %, 90 % and 100 %, respectively. Further hydrolytic potential of commercial cellulases viz. Accellerase™ 1,000, Palkofeel-30 and Palkocel-40 were investigated under similar conditions.

Effect of alkali pretreatment on the structural properties and enzymatic hydrolysis of corn cob.

Hexavalent chromium, which is a mutagen and carcinogen, was efficiently reduced by Streptomyces griseus. This activity was associated with the cell. Cr(6+) reduction by free as well as immobilized cells was studied: cells in PVA-alginate had the highest (100%) Cr(6+) removal efficiency in 24 h with reduction rates similar to free cells. Immobilized cells completely reduced 25 mg Cr(6+) l(-1) in 24 h. PVA-alginate immobilized cells could be reused four times to completely reduce 25 mg Cr(6+) l(-1) in 24 h each time. Chromate in a simulated effluent containing Cu(2+), Mg(2+), Mn(2+) and Zn(2+) was completely reduced by PVA-alginate immobilized cells within 9 h.

Hexavalent chromate reduction by immobilized Streptomyces griseus

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