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Thangamani Rajesh,Yung-Hun Yang,박형연,Eunjung Song,Changmin Sung,Sung-Hee Park,Jae-Hun Lee,Dongwon Yoo,김윤곤,전종민,김병기 한국화학공학회 2013 Korean Journal of Chemical Engineering Vol.30 No.2
Multidimensional protein identification technology (MudPIT) is one of the most versatile methods for separating and identifying highly complex peptides or proteins. However, there are still inherent problems resulting from salt in eluent systems and instrumentation with MudPIT. We designed a novel and simple flow path using twovalve system and successfully performed a fully automated peptide analysis using MudPIT coupled with nano-liquid chromatography electrospray ionization mass spectrometry (nLC-ESI-MS). It enables to generate a remarkably stable nanospray during the MudPIT analysis and realize the fully automated MudPIT system. This column arrangement could be easily installed to avoid laborious loading steps and unstable ionization from discontinuous flow. Consequently,the new flow path design for MudPIT system guarantees the detection of more peptides and higher protein coverage in proteome analysis.
Rajesh, Thangamani,Kim, Yong Hyun,Choi, Yong-Keun,Jeon, Jong Min,Kim, Hyun Joong,Park, Sung-Hee,Park, Hyung-Yeon,Choi, Kwon-Young,Kim, Hyungsup,Kim, Hyung Joo,Lee, Sang Hyun,Yang, Yung-Hun Humana Press 2013 Applied biochemistry and biotechnology Vol.170 No.2
<P>Amylases are important industrial enzymes that have been applied widely in the food, detergent, and pulp industries and fermentation processes. In the present study, a gene encoding an alpha-amylase from the genomic DNA library of Paenibacillus sp. was identified and characterized. The amylase gene designated amy1 was shown to consist of 1,980?bp and shared sequence identity towards α-amylase genes from other Bacillus sp. The deduced amino acid sequence for Amy1 indicated 80?% sequence identity with other Bacillus strains. Heterologous expression of recombinant Amy1 in Escherichia coli BL21(DE3) facilitated the recovery of this protein in soluble form. Enzyme kinetic data revealed Amy1 to have a K m of 23.83?mg/mL and K cat of 48.74?min(-1) and K cat /K m of 2?min(-1)?mg(-1)?mL(-1) for starch. The activity of this protein was found to be enhanced by Mn(2+), and furthermore, Amy1 remained active at a broad pH range (4-10) and temperature (30-90?C). The ability of Amy1 to act on food waste under broad temperature and pH conditions, together with its ability to produce simple sugars, shows many advantages for further application in the food industry.</P>
Rajesh, Thangamani,Song, Eunjung,Kim, Ji-Nu,Lee, Bo-Rahm,Kim, Eun-Jung,Park, Sung-Hee,Kim, Yun-Gon,Yoo, Dongwon,Park, Hyung-Yeon,Choi, Yun-Hui,Kim, Byung-Gee,Yang, Yung-Hun Springer International 2012 Applied microbiology and biotechnology Vol.93 No.4
<P>Phosphomannose isomerases (PMIs) in bacteria and fungi catalyze the reversible conversion of d-fructose-6-phosphate to d-mannose-6-phosphate during biosynthesis of GDP-mannose, which is the main intermediate in the mannosylation of important cell wall components, glycoproteins, and certain glycolipids. In the present study, the kinetic parameters of PMI from Streptomyces coelicolor were obtained, and its function on antibiotic production and sporulation was studied. manA (SCO3025) encoding PMI in S. coelicolor was deleted by insertional inactivation. Its mutant (S. coelicolora dagger manA) was found to exhibit a bld-like phenotype. Additionally, S. coelicolora dagger manA failed to produce the antibiotics actinorhodin and red tripyrolle undecylprodigiosin in liquid media. To identify the function of manA, the gene was cloned and expressed in Escherichia coli BL21 (DE3). The purified recombinant ManA exhibited PMI activity (K (cat)/K (m) (mM(-1) s(-1) = 0.41 for d-mannose-6-phosphate), but failed to show GDP-d-mannose pyrophosphorylase [GMP (ManC)] activity. Complementation analysis with manA from S. coelicolor or E. coli resulted in the recovery of bld-like phenotype of S. coelicolora dagger manA. SCO3026, another ORF that encodes a protein with sequence similarity towards bifunctional PMI and GMP, was also tested for its ability to function as an alternate ManA. However, the purified protein of SCO3026 failed to exhibit both PMI and GMP activity. The present study shows that enzymes involved in carbohydrate metabolism could control cellular differentiation as well as the production of secondary metabolites.</P>
Increased Sensitivity to Chloramphenicol by Inactivation of manB in Streptomyces coelicolor
( Rajesh Thangamani ),( Eun Jung Song ),( Bo Rahm Lee ),( Sung Hee Park ),( Jong Min Jeon ),( Eun Jung Kim ),( Chang Min Sung ),( Jae Hun Lee ),( Dong Won Yoo ),( Hyung Yeon Park ),( Yun Gon Kim ),( B 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.10
Phosphomannomutase (ManB) is involved in the biosynthesis of GDP-mannose, which is vital for numerous processes such as synthesis of carbohydrates, production of alginates and ascorbic acid, and post-translational modification of proteins. Here, we discovered that a deletion mutant of manB (BG101) in Streptomyces coelicolor (S. coelicolor) showed higher sensitivity to bacteriostatic chloramphenicol (CM) than the wild-type strain (M145), along with decreased production of CM metabolites. Deletion of manB also decreased the mRNA expression level of drug efflux pumps (i.e., cmlR1 and cmlR2) in S. coelicolor, resulting in increased sensitivity to CM. This is the first report on changes in antibiotic sensitivity to CM by deletion of one glycolysis-related enzyme in S. coelicolor, and the results suggest different approaches for studying the antibioticresistant mechanism and its regulation.
Manoharan, Gomathi,Sairam, Thiagarajan,Thangamani, Rajesh,Ramakrishnan, Dhivya,K.Tiwari, Manish,Lee, Jung-Kul,Marimuthu, Jeya IPC Science and Technology Press 2019 Enzyme and microbial technology Vol.131 No.-
<P><B>Abstract</B></P> <P>Endophytic fungi provide benefits to host plants by producing a diverse class of secondary metabolites (natural products). Arrays of polyketide natural products are synthesized by specific classes of polyketide synthases (PKS I, II and III) in host organisms. In the present study, we attempt to screen and identify type III PKSs in culturable fungal endophytes isolated from the ethno medicinal plants including <I>Arbus precatorius</I>, <I>Bacopa monnieri,Citrus aurantifolia</I> and <I>Datura metel</I> to detect the genetic potential of endophytic fungi in producing bioactive compounds. A total of seventeen endophytic fungal strains belonging to eight genera were identified using fungal morphology and rDNA-ITS phylogenetic analyses. A CODEHOP-PCR based strategy was followed to design degenerate primers for the screening of type III PKS genes from fungal endophytes. We had successfully amplified partial PKS genes from eight endophytes. The amplified PKS sequences showed 60–99% identity to already characterized/putative PKS genes. From the partial sequence of FiPKS from <I>Fusarium incarnatum</I> BMER1, a full-length gene was amplified, cloned and characterized. FiPKScDNA was cloned and expressed in <I>E. coli</I> Lemo21 (DE3) and the purified protein was shown to produce pyrones and resorcinols using acyl-CoA thioesters as substrates. FiPKS showed the highest catalytic efficiency of 7.6 × 10<SUP>4</SUP> s<SUP>−1</SUP> M<SUP>-1</SUP> with stearoyl CoA as a starter unit. This study reports the identification and characterization of type III PKS from endophytes of medicinal plants by CODEHOP PCR.</P> <P><B>Highlights</B></P> <P> <UL> <LI> A CODEHOP PCR based screening method was employed for type III polyketide synthase gene identification in fungal endophytes. </LI> <LI> By this approach, partial type III PKS genes from eight fungal endophytes were amplified and sequenced. </LI> <LI> FiPKS gene from Fusarium incarnatum BMER1, an endophyte of Bacopa monnieri was cloned and functionally characterized. </LI> <LI> FiPKS produced pyrones and resorcinols with the highest catalytic efficiency of 7.6 x 104 s-1 M-1towards stearoyl CoA. </LI> </UL> </P>