Biological Synthesis of Gold Nanoparticles by Fungus <Emphasis Type=Italic>Epicoccum</Emphasis><Emphasis Type=Italic>nigrum</Emphasis>

Gold nanoparticles exhibit unique optical, thermal, chemical and physical properties. The microorganisms have high potential for production of nanoparticles with wide applications. Application of fungi to produce nanoparticles is potentially exciting because of their ability to secrete large amounts of enzymes. In this study, we investigated biosynthesis of gold nanoparticles by the fungus Epicoccum nigrum isolated from Andalian gold mine in north-west of Iran. The gold nanoparticles were produced intra and extracellular by reaction of an aqueous solution of chloroauric acid with the biomass of fungus E. nigrum. The produced gold nanoparticles were in the size range of 5–50 nm in spherical and rod shapes. This is the first report on the biosynthesis of gold nanoparticles by the fungus E. nigrum.     

Reaction of methylpheophorbides <Emphasis Type=Italic>d</Emphasis> and <Emphasis Type=Italic>b</Emphasis> with amines

A series of formyl analogs of chlorin e₆ 13-amides were synthesized in high yields by reaction under mild conditions of primary and secondary amines with methylpheophorides b and d. In contrast with the secondary 13-amides, tertiary 13-amides were found as two isomers differing in the orientation of the amide plane relative to the plane of the chlorin ring. Methylpheophorbides b and d were more reactive toward the amines than methylpheophorbide a.     

Comparative characteristics of water-soluble proteins from <Emphasis Type=Italic>Larix sibirica</Emphasis>, <Emphasis Type=Italic>Picea obovata</Emphasis>, and <Emphasis Type=Italic>Abies sibirica</Emphasis> bud meristem

The amount of water-soluble proteins in bud meristem of Larix sibirica L., Picea obovata L., and Abies sibirica L. was shown to increase by 2-3 times in autumn during development of low-temperature resistance. The fractional composition of water-soluble proteins of the studied species and the amino-acid composition of groups of water-soluble proteins with different molecular weight (MW) were similar. Nitrogen accumulated as aspartic acid, glycine, and alanine in high- and medium-molecular-weight proteins. The peptides (MW < 5 kDa) typically had a high content of hydrophobic proline and hydrophilic tyrosine.