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Applications of Nanoagrochemicals
Published in Bhupinder Singh, Om Prakash Katare, Eliana B. Souto, NanoAgroceuticals & NanoPhytoChemicals, 2018
Nitin Kumar Singhal, Vishal Singh, Shimayali Kaushal
Nanosized sulfur nanoparticles have been discovered to be very efficient in inhibiting the progression of fungal species such as Fusarium solanii and Venturia inaequalis, responsible for causing Fusarium wilt disease and apple scab disease, respectively. Sulfur NPs have fungicidal efficacy, mainly via their accumulation on the cell wall and its consequent destruction (Jampílek and KráL'Ová, 2015). Overall lipid amount of the treated fungal species, such as Aspergillus niger, by spherical and cylindrical sulfur NPs resulted in the marked lowering of the expression of vital enzymes such as desaturases (linoleoyl-CoA desaturase, stearoyl-CoA 9-desaturase, and phosphatidylcholine desaturase). Also, increase in buildup of saturated fatty acids and worn-out lipid layers can be considered to be major factors of sulfur NP-enabled mycostasis. Besides inhibitory effects of sulfur NPs on fungal development and sporulation of A. niger and Fusarium oxysporum, they can also considerably decrease the phospholipid content (Roy Choudhury et al., 2011).
Identification and characterization of candidates involved in production of OMEGAs in microalgae: a gene mining and phylogenomic approach
Published in Preparative Biochemistry and Biotechnology, 2018
Vikas U. Kapase, Asha A. Nesamma, Pannaga P. Jutur
Various physico-chemical properties such as molecular weight, amino acid composition, stability, aliphatic index, and hydrophobicity were calculated using ExPASy’s ProtParam tool (Figure 3).[26,27] The molecular weight of OMEGA biosynthetic proteins ranges between 7183.22 and 171893.5 Da. It was observed that predicted pI values for all OMEGA proteins were basic in nature especially for 3-oxoacyl-[acyl-carrier-protein] reductase, stearoyl-CoA 9-desaturase, δ-12 desaturase, enoyl-CoA hydratase, acetyl-CoA acyltransferase, trans-2-enoyl-CoA reductase, acyl-CoA thioesterase, and 3-hydroxyacyl-CoA dehydratase; however, only acyl-CoA oxidase seems to be acidic in nature. The pI of the protein is significant in developing a buffer system during protein purification of the enzymes. Instability index helps us to distinguish between stable and unstable proteins by identifying the presence of certain dipeptides. The in vivo half-life of proteins can also co-related with instability index, indicating that the proteins with in vivo half-life >5 h have an instability index more than 40 and are assumed to be unstable whereas those with in vivo half-life >16 h have an instability index less than 40 and are predicted to be stable. The instability index of few proteins calculated was unstable and the reason may be due to inherent feedback mechanism that regulates the accumulation of cellular metabolites at optimal levels.[47] Our data show that δ-12 desaturase, acetyl-CoA acyltransferase, enoyl-CoA hydratase, and 3-oxoacyl-[acyl-carrier-protein] reductase are stable (Figure 3). The aliphatic index is directly related to the mole fraction of aliphatic side chains in the protein (alanine, isoleucine, leucine, and valine), and it will serve as a measure of thermostability in proteins. The aliphatic index of these proteins is within the range of 71.15–105.6. The presence of very high aliphatic index determines that their protein structures will be more stable at different ranges of temperatures.[40] The GRAVY index is the measure of solubility that indicates the nature of the protein. The increasing positive score indicates a greater hydrophobicity while negative score indicates hydrophilic in nature. In the present study, it was shown that 3-oxoacyl-[acyl-carrier-protein] reductase, 3-hydroxyacyl-CoA dehydratase, trans-2-enoyl-CoA reductase, and acetyl-CoA acyltransferase are hydrophobic, while others are hydrophilic in nature (Figure 3).