Protease from psychrotrophs: An overview

Not AvailableProteases are hydrolytic enzymes which catalyze the total hydrolysis of proteins in to amino acids. Although proteolytic enzymes can be obtained from animals and plants but microorganisms are the preferred source for industrial applications in view of scientific and economical advantage. Among various groups of microbes, psychrotrophs are ideal candidates for enzymes production keeping in mind that enzymes active at low temperature and stable under alkaline condition, in presence of oxidants and detergents are in large demand as laundry additive. The proteases from psychrotrophs also find application in environmental bioremediation, food and molecular biology. During the previous two decades, proteases from psychrotrophs have received increased attention because of their wide range of applications, but the full potential of psychrotrophic proteases has not been exploited. This review focuses attention on the present status of knowledge on the production, optimization, molecular characteristics, applications, substrate specificity, and crystal structure of psychrotrophic proteases. The review will help in making strategies for exploitation of psychrotrophic protease resources and improvement of enzymes to obtain more robust proteases of industrial and biotechnological significance.Not Availabl

Purification and characterization of an extracellular low temperature-active and alkaline stable peptidase from psychrotrophic Acinetobacter sp MN 12 MTCC (10786).

Not AvailableAn extracellular low temperature-active alkaline stable peptidase from Acinetobacter sp. MN 12 was purified to homogeneity with a purification fold of 9.8. The enzyme exhibited specific activity of 6,540 U/mg protein, with an apparent molecular weight of 35 kDa. The purified enzyme was active over broad range of temperature from 4 to 60 C with optimum activity at 40 C. The enzyme retained more than 75 % of activity over a broad range of pH (7.0–11.0) with optimum activity at pH 9.0. The purified peptidase was strongly inhibited by phenylmethylsulfonyl fluoride, giving an indication of serine type. The Km and Vmax for casein and gelatin were 0.3529, 2.03 mg/ml and 294.11, 384.61 lg/ml/min respectively. The peptidase was compatible with surfactants, oxidizing agents and commercial detergents, and effectively removed dried blood stains on cotton fabrics at low temperature ranging from 15 to 35 C.Not Availabl

Soil microbial diversity in drylands

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Heterologous expression and characterization of detergent stableendoglucanase EG5B from Paenibacillus sp. IHB B 3084

Not AvailabletThe endoglucanase gene EG5B of 1611 bp with a predicted molecular weight of 58.6 kDa from Paenibacillussp. IHB B 3084 was cloned and expressed in Escherichia coli BL21(DE3). The analysis of deduced amino acidsequence revealed a modular structure of the endoglucanase EG5B with an N-terminal catalytic domainof glycosyl hydrolase family 5 and a C-terminal carbohydrate-binding module of family 3. The purifiedenzyme showed high hydrolytic activity on carboxymethylcellulose, low activity on p-nitrophenyl -d-cellobioside, avicel and filter paper, and no activity on microcrystalline cellulose, p-nitrophenyl -d-glucoside, cellobiose and salicin as substrates. The enzyme was mild-alkaline active with optimum activity at pH 7–8 and stable over broad pH range. The temperature optimum was at 50◦C with >50%activity over 30–60◦C. The enzyme stability with >63% residual activity towards non-ionic and anionic surfactants and commercial detergents suggested its compatibility as an additive to detergents.Not Availabl

Microbial proteases: Detection, production and genetic improvement.

Not AvailableMicrobial proteases are one of the important groups of industrially and commercially produced enzymes contributing approximately 2/3 of all enzyme sales. Though proteases are produced by many microorganisms, emphasis is on the microorganisms producing proteases with desired characters. As demand for novel proteases is increasing day by day the initial screening methods and assays for protease detection are of utmost importance. This review focuses attention on present status of knowledge on the various methods and protocols available for protease screening, detection, and quantification starting from plate assays to spectrophotometric, fluorometric, and nanoparticles based assays. The review will help in making strategies for exploitation of protease resources and improvement of enzymes to obtain more robust proteases.Not Availabl

Copper Nanoparticles in Agriculture: Biological Synthesis and Antimicrobial Activity

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Cloning and expression of low temperature active endoglucanaseEG5C from Paenibacillus sp. IHB B 3084

Not AvailabletThe endoglucanase gene designated as EG5C encoding cold active endoglucanase produced by Paenibacil-lus sp. IHB B 3084 was cloned and expressed in Escherichia coli BL21(DE3). The gene consisting of 1719 bpopen reading frame encoded a protein of 573 amino acids with a predicted molecular weight of 63.5 kDa.The presence of N-terminal catalytic domain of the glycosyl hydrolase family 5 (GH5) and C-terminalcarbohydrate binding X2 domain suggested the modular nature of the enzyme. The native signal peptideof EG5C was capable of efficiently secreting the enzyme with near equal activities in the cytoplasmic andextracellular fractions. The recombinant enzyme purified 9.46 fold to homogeneity with 22.33% yieldgave 7.758 IU/mg specific activity. The enzyme was stable over the broad pH range of 4–12 with morethan 50% residual activity. The optimal activity was at 40◦C with 70% relative activity at 5◦C. The lowtemperature activity despite the shorter linker region suggested a novel cold adaptation mechanism bythe enzyme. The enzyme displayed higher activity on carboxymethylcellulose than avicel which is usefulin maintaining the tensile strength of fiber. The efficient secretion and low temperature activity offerprospect for large-scale production and industrial application of the endoglucanase

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Enhancing crop productivity through soil and nutrient management

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Not AvailableCopper nanoparticles have improved properties compared to the bulk copper material. Copper nanoparticles indeed find applications in gas sensors, heat transfer fluids, catalysis, solar energy and batteries. Antibacterial and antifungal activities of copper nanoparticles find applications in the agriculture and healthcare sectors. Nonetheless, careless use of copper nanoparticles may cause environmental pollution and health effects. Here we review the biosynthesis of copper nanoparticles using plant materials, named phytosynthesis, and micro-organisms. We also discuss the effect of copper nanoparticles on crops and pathogenic micro-organisms. Copper nanoparticles varying in sizes from 5 to 295 nm have been synthesized using leaf extracts and latex from plants, and using bacteria and fungi. Biosynthesized copper nanoparticles show good antimicrobial activity inhibiting the growth of pathogenic bacteria and pathogenic fungi. Copper nanoparticles enhance the germination and growth of some plants at lower concentrations, whereas high concentrations result in retarded growth. Keywords Copper nanoparticles Biosynthesis Antimicrobial activity Pathogenic micro-organisms Agriculture crops Phytosynthesis Introduction Increasing agriculture production in economized way without polluting the environment is a global challenge. Agriculture and healthcare sectors have witnessed great strides during recent past; still, many developing countries face the threat of food/healthcare insecurity (Husen and Siddiqi 2014). Exploiting the latest innovations in the field of nanobiotechnology, researchers are trying to develop alternative antimicrobial agents including cationic polymers, metal nanoparticles and antimicrobial peptides agains