Purification and properties of the highly thermostable alkaline protease from an alkaliphilic and thermophilic Bacillus sp.

1993 ◽  
Vol 30 (2) ◽  
pp. 245-256 ◽  
Author(s):  
N. Fujiwara ◽  
A. Masui ◽  
T. Imanaka
Keyword(s):  
Alkaline Protease ◽  
Bacillus Sp ◽  
Thermophilic Bacillus ◽  
Purification And Properties

Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16

1995 ◽  
Vol 43 (3) ◽  
pp. 473-481 ◽  
Author(s):  
T. Kobayashi ◽  
Y. Hakamada ◽  
S. Adachi ◽  
J. Hitomi ◽  
T. Yoshimatsu ◽  
...  
Keyword(s):  
Alkaline Protease ◽  
Bacillus Sp ◽  
Purification And Properties ◽  
Alkalophilic Bacillus

Purification and properties of extracellular endoxylanases from alkalophilic thermophilic Bacillus sp.

1992 ◽  
Vol 38 (5) ◽  
pp. 436-442 ◽  
Author(s):  
Devyani Dey ◽  
Jyoti Hinge ◽  
Abhay Shendye ◽  
Mala Rao
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Cross Reactivity ◽  
Bacillus Sp ◽  
Thermophilic Bacillus ◽  
Molecular Weights ◽  
Purification And Properties ◽  
Similar Temperature

An alkalophilic thermophilic Bacillus sp. (NCIM 59) isolated from soil produced two types of cellulase-free xylanase at pH 10 and 50 °C. The two enzymes (xylanase I and II) were purified to homogeneity by ethanol precipitation followed by Bio-Gel P-10 gel filtration and preparative polyacrylamide gel electrophoresis. The molecular weights of xylanase I and II were estimated to be 35 000 and 15 800, respectively, by sodium dodecyl sulfate gel electrophoresis. The enzymes exhibited immunological cross-reactivity and were glycoproteins. They had similar temperature (50–60 °C) and pH (6) optima. Both xylanases were stable at 50 °C at pH 7 for 4 days. However, xylanase I was comparatively more stable than xylanase II at 60 °C. The isoelectric points of xylanase I and II were 4 and 8, respectively. The apparent Km values, using xylan as substrate, were 1.58 and 3.5 mg/mL, and Vmax values were 0.0172 and 0.742 μmol∙min−1∙mg−1, respectively. Both xylanases were inhibited by N-bromosuccinimide, suggesting the involvement of tryptophan in the active site. The hydrolysis patterns demonstrated that the xylanases were endoenzymes. Xylanase I and II yielded mainly xylobiose, xylotriose, and higher xylooligosaccharides, with traces of xylose from xylan. Key words: cellulase-free xylanase, alkalophilic thermophilic Bacillus sp., enzyme purification, characterization.

Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16

1995 ◽  
Vol 43 (3) ◽  
pp. 473-481 ◽  
Author(s):  
T. Kobayashi ◽  
Y. Hakamada ◽  
S. Adachi ◽  
J. Hitomi ◽  
T. Yoshimatsu ◽  
...  
Keyword(s):  
Alkaline Protease ◽  
Bacillus Sp ◽  
Purification And Properties ◽  
Alkalophilic Bacillus

Enzymatic dehairing of goat skins using alkaline protease from Bacillus sp. SB12

2016 ◽  
Vol 121 ◽  
pp. 9-16 ◽  
Author(s):  
Selmen Briki ◽  
Olfa Hamdi ◽  
Ahmed Landoulsi
Keyword(s):  
Alkaline Protease ◽  
Bacillus Sp

scholarly journals Bacteriolytic Activity of Alkaline Protease BYA from Bacillus sp. Y

2005 ◽  
Vol 54 (11) ◽  
pp. 595-600 ◽  
Author(s):  
Seiichi TOBE ◽  
Toshiyuki WATANABE ◽  
Itsuo HAMA ◽  
Masanori IWAMA ◽  
Masachika IRIE
Keyword(s):  
Alkaline Protease ◽  
Bacillus Sp ◽  
Bacteriolytic Activity
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