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Mander, Poonam,Cho, Seung-Sik,Simkhada, Jaya Ram,Choi, Yun-Hee,Park, Da-Jeong,Ha, Jung-Wan,Yoo, Jin-Cheol 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.1
In an effort to identify a microbial lipase that can catalyze transesterification reactions used in biodiesel production, an organic solvent-tolerant lipase was purified from Streptomyces sp. CS268. The molecular weight of the purified lipase was estimated to be 37.5 kDa by SDS-PAGE. The lipase showed highest activity at a temperature of $30^{\circ}C$ and pH 8.0 while it was stable in the pH range 4.0 ~ 9.0 and at temperatures ${\leq}50^{\circ}C$. It showed the highest hydrolytic activity towards medium-length acyl chain p-nitrophenyl decanoate with $K_m$ and $V_{max}$ values of 0.59 mM and 319.5 mmol/mg/min, respectively. Also, the lipase showed non-position specificity for triolein hydrolysis. The purified lipase catalyzed transesterification reaction of soybean oil with methanol, suggesting that it can be a potential enzymatic catalyst for biodiesel production.
Mander, P.,Yoo, H. Y.,Kim, S. W.,Choi, Y. H.,Cho, S. S.,Yoo, J. C. HUMANA PRESS INC 2014 Applied biochemistry and biotechnology Vol.172 No.3
The aim of this present study was to produce a microbial enzyme that can potentially be utilized for the enzymatic transesterification of waste cooking oil. To that end, an extracellular lipase was isolated and purified from the culture broth of Streptomyces sp. CS273. The molecular mass of purified lipase was estimated to be 36.55 kDa by SDS PAGE. The optimum lipolytic activity was obtained at alkaline pH 8.0 to 8.5 and temperature 40 C, while the enzyme was stable in the pH range 7.0 similar to 9.0 and at temperature <= 40 degrees C. The lipase showed highest hydrolytic activity towards p-nitrophenyl myristate (C14). The lipase activity was enhanced by several salts and detergents including NaCl, MnSo(4), and deoxy cholic acid, while phenylmethylsulfonyl fluoride at concentration 10 mM inhibited the activity. The lipase showed tolerance towards different organic solvents including ethanol and methanol which are commonly used in transesterification reactions to displace alcohol from triglycerides (ester) contained in renewable resources to yield fatty acid alkyl esters known as biodiesel. Applicability of the lipase in transesterification of waste cooking oil was confirmed by gas chromatography mass spectrometry analysis.
A Novel Ca2+-Dependent Phospholipase D from Streptomyces tendae, Possessing Only Hydrolytic Activity
Poonam Mander,Jaya Ram Simkhada,조승식,Sung Ju Park,최홍석,Hei Chan Lee,송재경,유진철 대한약학회 2009 Archives of Pharmacal Research Vol.32 No.10
An extracellular phospholipase D (PLDSt) was purified from Streptomyces tendae by two successive chromatographic steps on Sepharose CL-6B and DEAE-Sepharose CL-6B. Molecular weight of the PLDSt was estimated to be approximately 43 kDa by sodium dodecyl sulfatepolyacrylamide gel electrophoresis. Maximal activity was at pH 8 and 60oC, and the enzyme was stable at or below 60oC and between pH 8 and 10, when assayed after 1.5 and 24 h, respectively. The enzyme activity had an absolute requirement of Ca2+, and the maximum activity was at 2 mM CaCl2. The Km and Vmax values for phosphatidyl choline were 0.95 mM and 810 μmol min-1 mg-1, respectively. More importantly, PLDSt could not catalyze transphosphatidylation of glycerol, L-serine, myo-inositol and ethanolamine, which have been extensively used to evaluate the activity. The result strongly suggests that PLDSt does not have the transphosphatidylation activity, thereby making it the first Streptomyces PLD possessing only hydrolytic activity. PLDSt may therefore be a novel type of PLD enzyme.
Poonam Mander,조승식,최윤희,Sandesh Panthi,최윤석,김환묵,유진철 대한약학회 2016 Archives of Pharmacal Research Vol.39 No.7
In an effort to identify a microbial enzyme thatcan be useful as a fungicide and biodegradation agent ofchitinous wastes, a chitinase (Chi242) was purified fromthe culture supernatant of Streptomyces anulatus CS242utilizing powder of shrimp shell wastes as a sole carbonsource. It was purified employing ammonium sulfate precipitationand gel permeation chromatography techniques. The molecular weight of the purified chitinase was*38 kDa by SDS-PAGE. The N-terminal amino acidsequence (A-P-G-A-P-G-T-G-A-L) showed close similarityto those of other Streptomyes chitinases. The purifiedenzyme displayed optimal activity at pH 6.0 and 50 Crespectively. It showed substantial thermal stability for 2 hat 30–60 C, and exhibited broad pH stability in the range5.0–13.0 for 48 h at 4 C. Scanning electron microscopyconfirmed the ability of this enzyme to adsorb onto solidshrimp bio-waste and to degrade chitin microfibers. Chi242could proficiently convert colloidal chitin to N-acetyl glucosamine(GlcNAc) and N-acetyl chitobiose (GlcNAc)2signifying that this enzyme is suitable for bioconversion ofchitin waste. In addition, it exerted an effective antifungalactivity towards fungal pathogen signifying its role as abiocontrol agent. Thus, a single microbial cell of Streptomycesanulatus CS242 justified its dual role.
Poonam Mander,조승식,Jaya Ram Simkhada,Yun Hee Choi,Da Jeong Park,Jung Wan Ha,유진철 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.1
In an effort to identify a microbial lipase that can catalyze transesterification reactions used in biodiesel production, an organic solvent-tolerant lipase was purified from Streptomyces sp. CS268. The molecular weight of the purified lipase was estimated to be 37.5 kDa by SDSPAGE. The lipase showed highest activity at a temperature of 30°C and pH 8.0 while it was stable in the pH range 4.0~ 9.0 and at temperatures ≤ 50°C. It showed the highest hydrolytic activity towards medium-length acyl chain pnitrophenyl decanoate with Km and Vmax values of 0.59 mM and 319.5 mmol/mg/min, respectively. Also, the lipase showed non-position specificity for triolein hydrolysis. The purified lipase catalyzed transesterification reaction of soybean oil with methanol, suggesting that it can be a potential enzymatic catalyst for biodiesel production.
Nafamostat mesilate negatively regulates the metastasis of triple-negative breast cancer cells
Sunam Mander,유동주,박수미,김동휘,용효정,김동식,Curie Ahn,김윤희,성재영,황종익 대한약학회 2018 Archives of Pharmacal Research Vol.41 No.2
Triple-negative breast cancer (TNBC) lacking ofoestrogen receptor, progesterone receptor, and epidermalgrowth factor receptor type 2 is a highly malignant diseasewhich results in a poor prognosis and rare treatmentoptions. Despite the use of conventional chemotherapy forTNBC tumours, resistance and short duration responseslimit the treatment efficacy. Therefore, a need exists todevelop a new chemotherapy for TNBC. The aim of thisstudy was to examine the anti-cancer effects of nafamostatmesilate (NM), a previously known serine protease inhibitorand highly safe drug on breast cancer cells. Here, weshowed that NM significantly inhibits proliferation,migration, and invasion in MDA-MB231 cells, induces G2/M phase cell-cycle arrest, and inhibits the expression ofcyclin-dependent kinase 1 (CDK1). Exposure of MDAMB231cells to NM also resulted in decreased transcriptionfactor activities accompanied by the regulated phosphorylationof signalling molecules and a decrease in metalloproteinases,the principal modulators of the extracellularenvironment during cancer progression. Especially, inhibitionof TGFb-stimulated Smad2 phosphorylation andsubsequent metastasis-related gene expression, and downregulationof ERK activity may be pivotal mechanismsunderlying inhibitory effects of NM on NM inhibits lungmetastasis of breast cancer cells and growth of colonizedtumours in mice. Taken together, our data revealed thatNM inhibits cell growth and metastasis of TNBC cells andindicated that NM is a multi-targeted drug that could be anadjunct therapy for TNBC treatment.