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G C, Pradeep,Yoo, Hah Young,Cho, Seung Sik,Choi, Yun Hee,Yoo, Jin Cheol Humana Press 2015 Applied biochemistry and biotechnology Vol.175 No.1
<P>Streptomyces sp. CS147 grown on chitin liquid medium incorporating 0.5 % colloidal chitin as a sole carbon source produced an extracellular chitinase (Ch147). The enzyme (Ch147) was purified using Sepharose CL-6B column chromatography and biochemically characterized. The enzymatic reaction products, analyzed using high-performance liquid chromatography and thin layer chromatography clearly indicates the production of N-acetyl-D-glucosamine (GlcNAc) as principal product which can be further hydrolyzed for the production of alcohol, a second generation biofuel. Ch147 hydrolyzed colloidal chitin to 0.278, 0.817, and 1.058 mg/mL of (GlcNAc) as a major product, at retention time of 4.3, respectively, when incubated for 8, 16, and 24 h at 50 °C. GlcNAc is a monosaccharide that usually polymerize linearly through (1, 4) 관 linkage. The 41 kDa molecular mass chitinase, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), has the amino acid sequences DINGGGATLPQKLYL significantly different from other chitinase. Ch147 had K m and V max values of 2.05???±???5.3 mg/mL and 467.2???±???2.4 mmol/min, respectively. Further, the purified enzyme (5 U) inhibits the fungal phytopathogens belonging to the genera Fusarium and Aspergillus. We believe that Ch147 is a potential candidate for the conversion of waste materials into simple sugar for productions of biofuels and also can be used as an alternative option for biological control of plant pathogens being unfriendly to chemicals.</P>
An Alkaline and Metallo-protein Type Endo Xylanase from Streptomyces sp. CSWu-1
Md. Arifur Rahman,최연희,Pradeep G. C.,최윤석,최은주,조승식,송재경,유진철 한국생물공학회 2014 Biotechnology and Bioprocess Engineering Vol.19 No.2
An alkaline xylanase (XynWu-1) fromStreptomyces sp. CSWu-1 was isolated from the Koreansoil sample, purified and biochemically characterized. Theextracellular xylanase was purified 4.8 fold with a 16%yield using Sephadex G-50 followed by DEAE-Sepharose(fast flow) column chromatography. The molecular massof the enzyme was approximately 37 kDa estimated bySDS-PAGE and xylan zymography. N-terminal amino acidsequence of XynWu-1 was AINVLVAALX. The enzymewas found to be stable in a broad range of pH (7.0 ~ 13.0)and to 50°C and have an optimal pH and temperature of11.0 and 60°C, respectively. XynWu-1 activity was foundto be affected by Mn2+ ion with highest activity at 6 mMand produced xylose, xylobiose, and xylotetraose as majorhydrolyzed end products. It was found to degrade agrowaste materials like corncob and wheat bran by XynWu-1(2,000 U/g) as shown by electron microscopy. As beingstable in extreme alkaline pH, diverse peculiar biochemicalcharacteristics, and ability to produce oligosaccharide showsthat XynWu-1 has potential application in various bioindustrieslike probiotics, ethanol, etc.
An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501
Md. Arifur Rahman,최윤희,G. C. Pradeep,유진철 대한약학회 2014 Archives of Pharmacal Research Vol.37 No.12
A chitinase from Streptomyces sp. CS501 wasisolated from the Korean soil sample, purified by singlestepchromatography, and biochemically characterized. The extracellular chitinase (Ch501) was purified to 4.60fold with yield of 28.74 % using Sepharose Cl-6B column. The molecular mass of Ch501 was approximately 43 kDaas estimated by SDS-PAGE and zymography. The enzyme(Ch501) was found to be stable over a broad pH range(5.0–10.0) and temperature (up to 50 C), and have anoptimum temperature of 60 C. N-terminal sequence ofCh501 was AAYDDAAAAA. Intriguingly, Ch501 washighly sensitive to ammonium sulfate but it’s completelysuppressed activity was recovered after desalting out. TLCanalysis of Ch501 showed the production of N-acetyl Dglucosamine(GlcNAc) and Diacetylchitobiose (GlcNAc)2,as a principal hydrolyzed product. Ch501 shows antifungalactivity against Fusarium solani and Aspergillus brasiliensis,which can be used for the biological control offungus. As has been simple in purification, stable in a broadrange of pH, ability to produce oligosaccharides, andantifungal activity showed that Ch501 has potential applicationsin industries as for chitooligosaccharides productionused as prebiotics and/or for the biological control ofplant pathogens in agriculture.
A novel low molecular weight endo-xylanase from Streptomyces sp. CS628 cultivated in wheat bran.
Rahman, Md Arifur,Choi, Yun Hee,Pradeep, G C,Choi, Yoon Seok,Choi, Eun Joo,Cho, Seung Sik,Yoo, Jin Cheol Humana Press 2014 Applied biochemistry and biotechnology Vol.173 No.6
<P>An extracellular low molecular weight xylanase (Xyn628) from Streptomyces sp. CS628 was isolated from Korean soil sample, produced in wheat bran medium, purified, and biochemically characterized. Xyn628 was purified 4.8-fold with a 33.78?% yield using Sepharose CL-6B column chromatography. The purified xylanase was ~18.1?kDa estimated by SDS-PAGE and xylan zymography. N-terminal amino acid sequences of Xyn628 were AYIKEVVSRAYM. The enzyme was found to be stable in a broad range of pH (5.0-13.0) and up to 60?C and have optimal pH and temperature of pH?11.0 and 60?C, respectively. Xyn628 activities were remarkable affected by various detergents, chelators, modulators, and metal ions. The xylanase produced xylobiose and xylotriose as principal hydrolyzed end products from the xylan. It was found to degrade agro-waste materials like corn cob and wheat bran by Xyn628 (20?U/g) as shown by electron microscopy. As being simple in purification, low molecular weight, alkaline, thermostable, and ability to produce xylooligosaccharides show that Xyn628 has potential applications in bioindustries as a biobleaching agent or/and xylooligosaccharides production with an appropriate utilization of agro-waste.</P>
A Novel Low-molecular Weight Alkaline Mannanase from Streptomyces tendae
유하영,Pradeep G. C.,김승욱,박돈희,최연희,서주원,유진철 한국생물공학회 2015 Biotechnology and Bioprocess Engineering Vol.20 No.3
A novel, low-molecular weight, alkaline mannanase from Streptomyces tendae (MnSt) was purified to homogeneity and biochemically characterized. The extracellular mannanase was purified with 26.3% yield using a Sepharose Cl-6B column. The molecular mass of MnSt was approximately 24 kDa. MnSt was stable over a broad pH range (5 ~ 12.5), was thermally stable at 60°C, and functioned optimally at 50°C and a pH of 12.0. MnSt had Km and Vmax values of 0.05 ± 1 mg/mL and 439 ± 0.5mmol/min, respectively, using bean gum galactomannan as a substrate. The N-terminal sequence of MnSt was GWSVDAPYIAXQPFS. Thin layer chromatography (TLC) analysis of the MnSt hydrolysis products suggested that the major oligosaccharide produced was mannobiose. MnSt activity was remarkably affected by metal ions, modulators, chelators, and detergents. MnSt was simple to purify, had high thermal stability, was stable over a broad pH range, and produced mannooligosaccharides. MnSt has high potential for use as an industrial biocatalyst, particularly as a bio-bleaching agent or for oligosaccharide production.