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A lot of crops are destroyed by the phytopathogens such as fungi, bacteria, and yeast leading to economic losses to the farmers. Members of the Bacillus genus are considered as the factories for the production of biologically active molecules that are potential inhibitors of growth of phytopathogens. Plant diseases constitute an emerging threat to global food security. Many of the currently available antimicrobial agents for agriculture are highly toxic and nonbiodegradable and thus cause extended environmental pollution. Moreover, an increasing number of phytopathogens have developed resistance to antimicrobial agents. The lipopeptides have been tried as potent versatile weapons to deal with a variety of phytopathogens. All the three families of Bacillus lipopeptides, namely, Surfactins, Iturins and Fengycins, have been explored for their antagonistic activities towards a wide range of phytopathogens including bacteria, fungi, and oomycetes. Iturin and Fengycin have antifungal activities, while Surfactin has broad range of potent antibacterial activities and this has also been used as larvicidal agent. Interestingly, lipopeptides being the molecules of biological origin are environmentally acceptable.

Cancer is a serious concern at present. A large number of patients die each year due to cancer illnesses in spite of several interventions available. Development of an effective and side effects lacking anticancer therapy is the trending research direction in healthcare pharmacy. Chemical entities present in plants proved to be very potential in this regard. Bioactive phytochemicals are preferential as they pretend differentially on cancer cells only, without altering normal cells. Carcinogenesis is a complex process and includes multiple signaling events. Phytochemicals are pleiotropic in their function and target these events in multiple manners; hence they are most suitable candidate for anticancer drug development. Efforts are in progress to develop lead candidates from phytochemicals those can block or retard the growth of cancer without any side effect. Several phytochemicals manifest anticancer function and . This article deals with these lead phytomolecules with their action mechanisms on nuclear and cellular factors involved in carcinogenesis. Additionally, druggability parameters and clinical development of anticancer phytomolecules have also been discussed.

Lipases are a group of enzymes naturally endowed with the property of performing reactions in aqueous as well as organic solvents. The esterification reactions using lipase(s) could be performed in water-restricted organic media as organic solvent(s) not only improve(s) the solubility of substrate and reactant in reaction mixture but also permit(s) the reaction in the reverse direction, and often it is easy to recover the product in organic phase in two-phase equilibrium systems. The use of organic solvent tolerant lipase in organic media has exhibited many advantages: increased activity and stability, regiospecificity and stereoselectivity, higher solubility of substrate, ease of products recovery, and ability to shift the reaction equilibrium toward synthetic direction. Therefore the search for organic solvent tolerant enzymes has been an extensive area of research. A variety of fatty acid esters are now being produced commercially using immobilized lipase in nonaqueous solvents. This review describes the organic tolerance and industrial application of lipases. The main emphasis is to study the nature of organic solvent tolerant lipases. Also, the potential industrial applications that make lipases the biocatalysts of choice for the present and future have been presented.

Industrial discharges of untreated effluents into water bodies and emissions into air have deteriorated the quality of water and air, respectively. The huge amount of pollutants derived from industrial activities represents a threat for the environment and ecologic equilibrium. Phenols and halogenated phenols, polycyclic aromatic hydrocarbons (PAH), endocrine disruptive chemicals (EDC), pesticides, dioxins, polychlorinated biphenyls (PCB), industrial dyes, and other xenobiotics are among the most important pollutants. Peroxidases are enzymes that are able to transform a variety of compounds following a free radical mechanism, thereby yielding oxidized or polymerized products. The peroxidase transformation of these pollutants is accompanied by a reduction in their toxicity, due to loss of biological activity, reduction in the bioavailability, or the removal from aqueous phase, especially when the pollutant is found in water. The review describes the sources of peroxidases, the reactions catalyzed by them, and their applications in the management of pollutants in the environment.

Engine oil used in automobiles is a threat to soil and water due to the recalcitrant properties of its hydrocarbons. It pollutes surrounding environment which affects both flora and fauna. Microbes can degrade hydrocarbons containing engine oil and utilize it as a substrate for their growth. Our results demonstrated that cell-free broth of Bacillus velezensis KLP2016 (Gram + ve, endospore forming; Accession number KY214239) recorded an emulsification index (E 24 %) from 52.3% to 65.7% against different organic solvents, such as benzene, pentane, cyclohexane, xylene, n -hexane, toluene and engine oil. The surface tension of the cell-free broth of B. velezensis grown in Luria–Bertani broth at 35 °C decreased from 55 to 40 mN m −1 at critical micelle concentration 17.2 µg/mL. The active biosurfactant molecule of cell-free broth of Bacillus velezensis KLP2016 was purified by Dietheylaminoethyl-cellulose and size exclusion chromatography, followed by HPLC (RT = 1.130), UV–vis spectrophotometry (210 nm) and thin layer chromatography (R f  = 0.90). The molecular weight of purified biosurfactant was found to be ~ 1.0 kDa, based on Electron Spray Ionization-MS. A concentration of 1980 × 10 –2 parts per million of CO 2 was trapped in a KOH solution after 15 days of incubation in Luria–Bertani broth containing 1% engine oil. Our results suggest that bacterium Bacillus velezensis KLP2016 may promise a new dimension to solving the engine oil pollution problem in near future.

Lipopeptides are surface active molecules with hydrophilic and hydrophobic regions and are kenned to be engendered by different species of Bacillus and Pseudomonas. These lipopeptides can be applied in different domains because of their remarkable properties like antibacterial, antifungal, anticorrosion, antitumor, and antiviral. They act by engendering pores in the cell membrane to perforate and conclusively disrupt them. This property of lipopeptide is valuable as an antimicrobial agent. In 2003, lipopeptides were approved as an antibiotic drug in the United States by the USA Food and Drug Administration (FDA) for the purpose of skin and blood infections caused by bacterial species. The biosynthetic genes for these lipopeptides are regulated by the nonribosomal peptide synthetase system. Amphisin, Tolaasin, Viscosin, and Syringomycin are the four main types of lipopeptides produced by Pseudomonas species. Since these lipopeptides are nontoxic, biodegradable, and environmentally cordial, they can abbreviate undesirable ecological perturbances. They can be considered a multifarious weapon for their application in different domains such as biocontrol agents in plants, emulsifiers in cosmetic and food industries, anticorrosion agents in petroleum industries, and antimicrobial agents in pharmaceutical and biomedical industries. Lipopeptides are surface active molecules with hydrophilic and hydrophobic regions and are kenned to be engendered by different species of Bacillus and Pseudomonas. These lipopeptides can be applied in different domains because of their remarkable properties like antibacterial, antifungal, anticorrosion, antitumor, and antiviral. They act by engendering pores in the cell membrane to perforate and conclusively disrupt them.

Ascorbyl palmitate was synthesized using a Celite-immobilized commercial lipase (Lipolase 100L) in dimethylsulfoxide (DMSO) as an organic solvent system. Lipase immobilized by surface adsorption onto Celite 545 matrix and subsequently exposed to 1 % glutaraldehyde showed 75 % binding of protein. The Celite-bound lipase was optimally active at 75 °C and pH 8.5 under shaking and showed maximum hydrolytic activity toward p -NPP as a substrate. The bound lipase was found to be stimulated only in the presence of Al 3+ and EDTA. All surfactants (Tween-20, Tween-80 and Triton X-100) had an inhibitory effect on lipase activity. The optimization of various reaction conditions of ascorbyl palmitate was achieved considering one factor at a time. The esterification of ascorbic acid and palmitic acid was carried out with 1 M ascorbic acid and 2.5 M palmitic acid in DMSO at 75 °C for 18 h under shaking (120 rpm). Molecular sieves had an important effect on the ester synthesis resulting in an enhanced yield. The by-product (H 2 O) produced in the reaction was scavenged by the molecular sieves (20 mg/ml) added in the reaction mixture which enhanced the ester yield to 80 %. The characterization of synthesized ester was done through FTIR spectroscopy.

Surfactin lipopeptide (SLP) from Bacillus subtilis KLP2015 (Accession number KT459335) was extracted and purified by ammonium sulphate precipitation, DEAE and size exclusion chromatography. The molecular mass of the purified Surfactin lipopeptide was determined ~ 1000 Dalton through ESI-MS and MALDI-TOF-MS/MS analysis. The purified Surfactin possessed a strong cytotoxicity towards tested mammalian cancer cells HCT-15, Hep2-C, L-132, MCF-7 and NIH/3T3 with the percentage cell death of 80.1 ± 1.92%, 76.09 ± 1.32%, 88.56 ± 2.41%, 78.91 ± 2.09% and 77.84 ± 1.96% respectively and less cytotoxicity to normal HaCaT cells (31.45 ± 2.58%). A fivefold decrease in DNA content was noted in LP treated L-132 cells while twofold in Hep2-C after 20 h while, SDS treated L-132 and Hep2-C cells showed approximate 1.5 and 1.4-fold decrease in DNA content from its initial. The antibacterial assay using purified LP (concentration, 50 µg/well) of B. subtilis KLP2015 exhibited marked inhibtion of Klebsiella pnemoniae (15.0 ± 0.4 mm), Salmonella typhimurium NCTC 74 (13.0 ± 0.2 mm), Staphylococcus aureus ATCC 6538(12.0 ± 0.3 mm) and Escherichia coli NCTC 10418(8.0 ± 0.7 mm). The dislodging of biofilms formation was observed in all the 7 tested strains except Shigella flexneri. The maximum process of biofilm formation was reduced by 58% in case of S. aureus ATCC 6538.

Cancer is an increasing cause of mortality and morbidity throughout the world. L-methionase has potential application against many types of cancers. L-Methionase is an intracellular enzyme in bacterial species, an extracellular enzyme in fungi, and absent in mammals. L-Methionase producing bacterial strain(s) can be isolated by 5,5′-dithio-bis-(2-nitrobenzoic acid) as a screening dye. L-Methionine plays an important role in tumour cells. These cells become methionine dependent and eventually follow apoptosis due to methionine limitation in cancer cells. L-Methionine also plays an indispensable role in gene activation and inactivation due to hypermethylation and/or hypomethylation. Membrane transporters such as GLUT1 and ion channels like Na2+, Ca2+, K+, and Cl− become overexpressed. Further, the α-subunit of ATP synthase plays a role in cancer cells growth and development by providing them enhanced nutritional requirements. Currently, selenomethionine is also used as a prodrug in cancer therapy along with enzyme methionase that converts prodrug into active toxic chemical(s) that causes death of cancerous cells/tissue. More recently, fusion protein (FP) consisting of L-methionase linked to annexin-V has been used in cancer therapy. The fusion proteins have advantage that they have specificity only for cancer cells and do not harm the normal cells.

A mesophilic Bacillus sp. initially isolated from tiger excreta and later identified as a Bacillus subtilis strain was used to produce an extracellular cholesterol oxidase (COX) in cholesterol-enriched broth. This bacterial isolate was studied for the production of COX by manipulation of various physicochemical parameters. The extracellular COX was successfully purified from the cell-free culture broth of B. subtilis by successive salting out with ammonium sulfate, dialysis, and riboflavin-affinity chromatography. The purified COX was characterized for its molecular mass/structure and stability. The enzyme possessed some interesting properties such as high native Mr (105 kDa), multimeric (pentamer of ∼21 kDa protein) nature, organic solvent compatibility, and a half-life of ∼2 h at 37 °C. The bacterial COX exhibited ∼22 % higher activity in potassium phosphate buffer (pH 7.5) in the presence of a nonionic detergent Triton X-100 at 0.05 % (v/v). The K ₘ and V ₘₐₓ value of COX of B. subtilis COX were found to be 3.25 mM and 2.17 μmol min ml⁻¹, respectively. The purified COX showed very little cytotoxicity associated with it.