Expression and characterization of GH3 β-Glucosidase from Aspergillus niger NL-1 with high specific activity, glucose inhibition and solvent tolerance

Microbiology ◽  
2013 ◽  
Vol 82 (3) ◽  
pp. 356-363 ◽  
Author(s):  
Linguo Zhao ◽  
Tanche Zhou ◽  
Xun Li ◽  
Song Fan ◽  
Lijin You
Keyword(s):  
Aspergillus Niger ◽  
Specific Activity ◽  
High Specific Activity ◽  
Solvent Tolerance ◽  
Glucose Inhibition

Overexpression and characterization of a glucose-tolerant β-glucosidase from T. aotearoense with high specific activity for cellobiose

2015 ◽  
Vol 99 (21) ◽  
pp. 8903-8915 ◽  
Author(s):  
Fang Yang ◽  
Xiaofeng Yang ◽  
Zhe Li ◽  
Chenyu Du ◽  
Jufang Wang ◽  
...  
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Glucose Tolerant

scholarly journals KARAKTERISASI FISIKO-KIMIA RADIOISOTOP 149Pm HASIL IRADIASI BAHAN SASARAN 148Nd ALAM

2015 ◽  
Vol 16 (1) ◽  
pp. 29
Author(s):  
Azmairit Aziz ◽  
Nana Suherman
Keyword(s):  
Cancer Therapy ◽  
Radiochemical Purity ◽  
Specific Activity ◽  
High Specific Activity ◽  
Chemical Characterization ◽  
Irradiation Position ◽  
Radionuclide Purity ◽  
Physico Chemical ◽  
Carrier Free

ABSTRAK KARAKTERISASI FISIKO-KIMIA RADIOISOTOP 149Pm HASIL IRADIASI BAHAN SASARAN 148Nd ALAM. Penyakit kanker merupakan salah satu masalah utama yang dihadapi Indonesia di bidang kesehatan. Radioisotop pemancar-β- dengan aktivitas jenis tinggi dapat digunakan untuk penandaan biomolekul sebagai radiofarmaka spesifik target untuk terapi sel kanker. Promesium-149 (149Pm) merupakan salah satu radiolantanida pemancar-β- yang me-miliki energi beta (Eβ-)maksimum sebesar 1,07 MeV (95,9 %) dan dapat dipertimbangkan untuk digunakan pada terapi kanker berdasarkan sifat nuklir yang dimilikinya. Radioisotop 149Pm dapat dibuat dengan cara tidak langsung melalui reaksi inti (n,γ) di reaktor nuklir menggunakan bahan sasaran isotop 148Nd (neodymium-148) dan radioisotop 149Pm yang dihasilkan adalah bebas pengemban (carrier free) sehingga memiliki aktivitas jenis tinggi. Pada penelitian ini digunakan bahan sasaran Nd2O3 alam yang diiradiasi selama ± 4 hari di Central Irradiation Position (CIP) RSG-G.A.Siwabessy – Serpong pada fluks neutron termal ~1014 n.cm-2.det-1. Radioisotop 149Pm dipisahkan dari bahan sasaran Nd2O3 hasil iradiasi menggunakan metode kromatografi ekstraksi. Larutan radioisotop 149PmCl3 yang dihasilkan dikarakterisasi secara fisiko-kimia meliputi penentuan kemurnian radiokimia menggunakan metode kromatografi kertas dan elektroforesis kertas. Kemurnian radionuklida ditentukan menggunakan spektro-meter-γ dengan detektor HP-Ge yang dilengkapi multichannel analyzer (MCA). Larutan 149PmCl3 yang diperoleh berupa larutan jernih, memiliki pH 2 dan konsentrasi radioaktif 4,2 – 7,4 mCi/mL. Larutan 149PmCl3 memiliki kemurnian radiokimia 99,70 ± 0,23% dan kemurnian radionuklida setelah pendinginan selama 9 hari sebesar 98,58 ± 0,44%. Larutan 149PmCl3 stabil selama 2 minggu pada temperatur kamar. Larutan radioisotop 149PmCl3 memiliki karakteristik fisiko-kimia yang memenuhi persyaratan untuk digunakan dalam pembuatan radiofarmaka ABSTRACT  PHYSICO - CHEMICAL CHARACTERIZATION OF 149Pm RADIOISOTOPE FROM IRRADIATED NATURAL 148Nd TARGET. Cancer is one of the major problems encountered in the field of health in Indonesia. A beta-emitting radioisotope with high specific activity can be used for labeling of biomolecules as a targeted radiopharmaceutical for cancer therapy. Promethium-149 (149Pm) is one of beta-emitting radiolanthanides with beta energy (Eβ-) maximum of 1.07 MeV (95.9%) and can be considered to be used for cancer therapy based on its nuclear properties. Radioisotope of 149Pm can be produced by indirect methode through (n,γ) reaction in nuclear reactor using 148Nd (neodymium-148) target material and 149Pm was produced as a carrier free radioisotope, so that it has high specific activity. In this study, natural Nd2O3 target was irradiated for ± 4 days in central irradiation position (CIP) of RSG-G.A. Siwabessy – Serpong at a thermal neutron flux of ~ 1014 n.cm-2.sec-1. Radioisotope of 149Pm was separated from irradiated of Nd2O3 target using extraction chromatography method. The physico-chemical characterization of 149PmCl3 solution was studied involves the determination of its radiochemical purity using paper chromatography and paper electrophoresis methods. The radionuclide purity was determined using a γ-spectrometer with  HP-Ge detector and coupled with a multichannel analyzer (MCA). 149PmCl3 was obtained as a clear solution, has a pH of 2 and  radioactive concentration of 4.2 to 7.4 mCi/mL. 149PmCl3 solution has radiochemical purity of 99.70 ± 0.23% and radionuclide purity after cooling for 9 days of 98.58 ± 0.44%. 149PmCl3 solution was stable for 2 weeks at room temperature. 149PmCl3 solution has the physico-chemical characteristics that meet requirements for use in preparation of radiopharmaceuticals.

Purification and Partial Characterization of Cellulase Produced by Aspergillus niger Cultured on Vitellaria paradoxa shells

2017 ◽  
Vol 6 (2) ◽  
Author(s):  
Abdulhakeem Olarewaju Sulyman ◽  
Yusuf A Iyanda ◽  
Afolabi Olaniyi Opasola ◽  
OtunOla Adedayo ◽  
Raliat Abimbola Aladodo
Keyword(s):  
Aspergillus Niger ◽  
Specific Activity ◽  
Gel Filtration ◽  
Inoculum Size ◽  
Partial Characterization ◽  
Effect Of Temperature ◽  
Vitellaria Paradoxa ◽  
Endoglucanase Activity ◽  
Ammonium Sulphate Precipitation

This research investigated the purification and partial characterization of cellulase produced by Aspergillus niger cultured on Vitellaria paradoxa shells. Cellulase (endoglucanase) from A. niger was produced under optimum fermentation conditions at 35 °C, pH 4.7, V. paradoxa, 4 g/L, inoculum size of 10 mm and the fermentation media incubated for 120 hours. The crude endoglucanase obtained were partially purified by subjecting to ammonium sulphate precipitation, dialysis and gel filtration chromatography for further purification. The effect of temperature and pH on the activity of purified endoglucanase was determined. Cellulase was purified to 734.33 folds by Sephadex G-100 column chromatography with a specific activity and yield of 4.406 U/mg and 63.03% respectively. Fractions 4 and 7 contained the highest endoglucanase activity out of 18 fractions collected and the two fractions were pooled for further analysis. The activity of purified endoglucanase was optimum at a temperature of 40 °C and pH 5. Therefore, the purified endoglucanase produced may be explored in detergent industry.

Preparation and characterization of high-specific activity radiolabeled so S measles virus RNA

1980 ◽  
Vol 1 (4) ◽  
pp. 223-228 ◽  
Author(s):  
Spotswood L. Spruance ◽  
Bruce N. Ashton ◽  
Charles B. Smith
Keyword(s):  
Measles Virus ◽  
Specific Activity ◽  
High Specific Activity ◽  
Virus Rna

scholarly journals Thermostable Chitosanase from Bacillus sp. Strain CK4: Cloning and Expression of the Gene and Characterization of the Enzyme

2000 ◽  
Vol 66 (9) ◽  
pp. 3727-3734 ◽  
Author(s):  
Ho-Geun Yoon ◽  
Hee-Yun Kim ◽  
Young-Hee Lim ◽  
Hye-Kyung Kim ◽  
Dong-Hoon Shin ◽  
...  
Keyword(s):  
Gene Sequence ◽  
Specific Activity ◽  
High Specific Activity ◽  
Industrial Applications ◽  
Cloning And Expression ◽  
Rrna Gene ◽  
Phenotypic Analysis ◽  
Reading Frame ◽  
The 16S Rrna Gene

ABSTRACT A thermostable chitosanase gene from the environmental isolateBacillus sp. strain CK4, which was identified on the basis of phylogenetic analysis of the 16S rRNA gene sequence and phenotypic analysis, was cloned, and its complete DNA sequence was determined. The thermostable chitosanase gene was composed of an 822-bp open reading frame which encodes a protein of 242 amino acids and a signal peptide corresponding to a 30-kDa enzyme. The deduced amino acid sequence of the chitosanase from Bacillus sp. strain CK4 exhibits 76.6, 15.3, and 14.2% similarities to those from Bacillus subtilis, Bacillus ehemensis, and Bacillus circulans, respectively. C-terminal homology analysis shows thatBacillus sp. strain CK4 belongs to cluster III withB. subtilis. The gene was similar in size to that of the mesophile B. subtilis but showed a higher preference for codons ending in G or C. The enzyme contains 2 additional cysteine residues at positions 49 and 211. The recombinant chitosanase has been purified to homogeneity by using only two steps with column chromatography. The half-life of the enzyme was 90 min at 80�C, which indicates its usefulness for industrial applications. The enzyme had a useful reactivity and a high specific activity for producing functional oligosaccharides as well, with trimers through hexamers as the major products.

Sign in / Sign up

Export Citation Format

Share Document