Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents

2010 ◽  
Vol 101 (21) ◽  
pp. 8361-8369 ◽  
Author(s):  
Bassem Jaouadi ◽  
Badis Abdelmalek ◽  
Djamila Fodil ◽  
Fatma Zohra Ferradji ◽  
Hatem Rekik ◽  
...  
Keyword(s):  
Organic Solvents ◽  
High Stability ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Alkaline Proteinase

scholarly journals Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

Purification and characterization of a new 120 kDa alkaline proteinase of Trypanosoma cruzi

1992 ◽  
Vol 187 (3) ◽  
pp. 1466-1473 ◽  
Author(s):  
Jaime Martins Santana ◽  
Philippe Grellier ◽  
Marie-Hélène Rodier ◽  
Joseph Schrevel ◽  
Antonio Teixeira
Keyword(s):  
Trypanosoma Cruzi ◽  
Purification And Characterization ◽  
Alkaline Proteinase

Purification and characterization of a fibrinolytic enzyme from Streptomyces sp. XZNUM 00004

2012 ◽  
Vol 28 (7) ◽  
pp. 2479-2486 ◽  
Author(s):  
Xiuyun Ju ◽  
Xiaoying Cao ◽  
Yong Sun ◽  
Zhe Wang ◽  
Chengliang Cao ◽  
...  
Keyword(s):  
Fibrinolytic Enzyme ◽  
Purification And Characterization ◽  
Streptomyces Sp

Purification and characterization of four keratinases produced by Streptomyces sp. strain 16 in native human foot skin medium

2010 ◽  
Vol 101 (1) ◽  
pp. 344-350 ◽  
Author(s):  
Fuhong Xie ◽  
Yapeng Chao ◽  
Xiuqing Yang ◽  
Jing Yang ◽  
Zhiquan Xue ◽  
...  
Keyword(s):  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Human Foot
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