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פותח על ידי קלירמאש פתרונות בע"מ -
An alkali-halotolerant cellulase from Bacillus flexus isolated from green seaweed Ulva lactuca
Year:
2011
Source of publication :
Carbohydrate Polymers
Authors :
קומארי, פוג'ה
;
.
Volume :
83
Co-Authors:
Trivedi, N., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Gupta, V., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Kumar, M., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Kumari, P., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Reddy, C.R.K., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Jha, B., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Facilitators :
From page:
891
To page:
897
(
Total pages:
7
)
Abstract:
An extracellular alkali-halotolerant cellulase from the strain Bacillus flexus NT isolated from Ulva lactuca was purified to homogeneity with a recovery of 25.03% and purity fold of 22.31. The molecular weight of the enzyme was about 97 kDa and the Vmax and Km was 370.17 U/ml/min and 6.18 mg/ml respectively. The optimum pH and temperature for enzyme activity was 10 and 45 °C respectively. The enzymatic hydrolysis of the CMC was confirmed with GPC and GC-MS analysis. The stabilized activity of the enzyme even at high pH of 9.0-12.0 and residual activity of about 70% at salt concentration (NaCl 15%) revealed for its alkali-halotolerance nature. The metal ions Cd 2+ and Li1+ were found as inducers while Cr2+, Co2+, Zn2+ and metal chelator EDTA have significantly inhibited the enzyme activity. Enzyme activity was insensitive to ethanol and isopropanol while partially inhibited by acetone, cyclohexane and benzene. © 2010 Elsevier Ltd. All rights reserved.
Note:
Related Files :
acetone
Bacteriology
Benzene
ecosystems
enzymes
ethanol
Halo-alkali tolerance
Iso-propanols
Marine habitat
Ocean habitats
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.carbpol.2010.08.069
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
24993
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:11
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Scientific Publication
An alkali-halotolerant cellulase from Bacillus flexus isolated from green seaweed Ulva lactuca
83
Trivedi, N., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Gupta, V., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Kumar, M., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Kumari, P., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Reddy, C.R.K., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
Jha, B., Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific and Industrial Research (CSIR), Bhavnagar 364021, India
An alkali-halotolerant cellulase from Bacillus flexus isolated from green seaweed Ulva lactuca
An extracellular alkali-halotolerant cellulase from the strain Bacillus flexus NT isolated from Ulva lactuca was purified to homogeneity with a recovery of 25.03% and purity fold of 22.31. The molecular weight of the enzyme was about 97 kDa and the Vmax and Km was 370.17 U/ml/min and 6.18 mg/ml respectively. The optimum pH and temperature for enzyme activity was 10 and 45 °C respectively. The enzymatic hydrolysis of the CMC was confirmed with GPC and GC-MS analysis. The stabilized activity of the enzyme even at high pH of 9.0-12.0 and residual activity of about 70% at salt concentration (NaCl 15%) revealed for its alkali-halotolerance nature. The metal ions Cd 2+ and Li1+ were found as inducers while Cr2+, Co2+, Zn2+ and metal chelator EDTA have significantly inhibited the enzyme activity. Enzyme activity was insensitive to ethanol and isopropanol while partially inhibited by acetone, cyclohexane and benzene. © 2010 Elsevier Ltd. All rights reserved.
Scientific Publication
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