Development of Specific Primer for Tricholoma matsutake

In this study, in an effort to develop a method for the molecular detection of Tricholoma matsutake in Korea from other closely related Tricholomataceae, a species-specific PCR primer pair, TmF and TmR, was designed using nuclear ribosomal intertranscribed spacer (ITS) sequences. The DTmF and DTmR sequences were 5'-CCTGACGCCAATCTTTTCA-3' and 5'-GGAGAGCAGACTTGTGAGCA-3', respectively. The PCR primers reliably amplified only the ITS sequences of T. matsutake, and not those of other species used in this study.

Cultural Characteristics for the Enhanced Mycelial Growth of Ramaria botrytis

The culture conditions for the enhanced mycelial growth of Ramaria botrytis was investigated. The optimal temperature and pH for the mycelial growth were 24degrees C and 5.0, respectively. It was shown that starch was best of several carbon sources in Czapek-Dox medium as a minimal medium for the enhanced mycelial growth. Organic nitrogen sources were better than inorganic ones for mycelial growth. The appropriate vitamin and mineral salt were biotin and FeCl3, respectively. When this strain was cultured with FeCl3 for 30 days, 19.23 g/l of dry mycelium of R. botrytis was obtained.

Cytotoxicity of Paecilomyces tenuipes Against Human Carcinoma Cells, HepG2 and MCF-7 In Vitro

The methanolic extract of fruiting body of Paecilomyces tenuipes DGUM 32001 showed significant cytotoxicity against human cancer cells: HepG2 and MCF-7. The methanolic extract was further fractionated with organic solvents such as chloroform and ethyl acetate in that order. Among the fractions tested, the ethyl acetate fraction showed the highest cytotoxicity against the carcinoma tested. The IC50 values of ethyl acetate fraction against HepG and MCF-7 were 40 and 9.6 microg/ml, respectively.

Enzyme Activities of the Fruit Body of Ramaria botrytis DGUM 29001

The fruit body of Ramaria botrytis DGUM 29001 was used to determine enzyme activities of fruit body. The specific activity of laccase was the highest(6.5 unit/mg.protein) and that of alpha-amylase and xylanase was relatively high. However, little or no enzyme activity of beta-glucosidase, CMCase, exo-beta-1,4-glucanase, chitinase, lipase and protease was found.

Cloning and Nucleotide Sequence of Streptococcus pneumoniae ftsH Gene

The gene ftsH encodes a membrane-bound and ATP-dependent protease that is involved in a variety of cellular functions including heat-shock and stress response. Streptococcus pneumoniae DNA encompassing most part of the ftsH gene was cloned in Escherichia coli and sequenced. Due to the unsuccessful cloning as seen in other pneumococcal promoters, the 5'-end of the gene including the upstream promoter region was amplified by inverse polymerase chain reaction and then sequenced by cyclic sequencing. The amino acid sequence that is deduced from the 1,959 bp-long ftsH gene is very similar to FtsH of several gram-positive bacteria and E. coli within the region responsible for the AAA (ATPase associated with diverse cellular activities) function. Except for the N-terminal domain that contains a short extracellular region between two mernbrane-spanning segments, pneumococcal FtsH shows striking sequence similarity to that of a closely related species Lactococcus lactis within the conserved cytoplasmic domain where two ATP-binding motifs, the AAA Signature motif, and a zinc-binding motif are found.