EXPRESSION AND CHARACTERIZATION OF BACTERIAL ORGANOPHOSPHORUS HYDROLASE IN PICHIA PASTORIS WITH THE INTENT TO DEGRADE ORGANOPHOSPHATE NEUROTOXINS

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

NAJAVAND SAEED; SAHEBGHADAM LOTFI ABBASS; MOHSENIFAR AFSHIN; ARJMAND SAREH; MOTA ALI

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Pathobiology Research Year:2012 | Volume:15 | Issue:1 Page(s): 61-72

Download Full-Text

Persian Verion

View:

1,428

Download:

Cites:

Information Journal Paper

Title

EXPRESSION AND CHARACTERIZATION OF BACTERIAL ORGANOPHOSPHORUS HYDROLASE IN PICHIA PASTORIS WITH THE INTENT TO DEGRADE ORGANOPHOSPHATE NEUROTOXINS

Author(s)

Keywords

ORGANOPHOSPHORUS COMPOUNDSQ2

ORGANOPHOSPHORUS HYDROLASEQ2

PICHIA PASTORISQ3

Abstract

Objective: ORGANOPHOSPHORUS HYDROLASE (OPH) is a homodimeric enzyme that can hydrolyze phosphoester bonds and reduce the toxicity of ORGANOPHOSPHORUS COMPOUNDS. This makes OPH a suitable element for the biodegradation of these compounds.Methods: We successfully cloned the OPH gene from Pseudomonas diminuta, after optimization for PICHIA PASTORIS, into a yeast expression vector (pPICZaB). After transformation and induction of recombinant yeasts, the expressed enzyme was investigated for its biochemical and kinetical parameters.Results: The enzyme was purified 7.49-fold to a specific activity of 0.421×103 U/mg protein from the supernatant with a yield of 33%. The purified enzyme was able to degrade organophosphates. It had an optimal activity and stability up to 50oC, and a pH range of 7.0-10.0. The enzyme had a Km of 45.96 mM and a Vmax of 11.23 mM/min (421 mM/min/mg) for paraoxon as a substrate. This enzyme was sensitive to divalent cations and inactivated by denaturing compounds such as SDS. The molecular mass of the purified enzyme as estimated by SDS–PAGE analysis was approximately 40 kDa. Conclusion: In this study, the purified enzyme effectively hydrolyzed paraoxon, an organophosphorus compound. The activity and stability of this enzyme at high temperatures and pH, and low Km in comparision with bacterial isolates could make it an attractive biocatalyst for applied bioremediation and bio sensing.

Cites

No record.

References

No record.

Cite

APA: Copy

NAJAVAND, SAEED, SAHEBGHADAM LOTFI, ABBASS, MOHSENIFAR, AFSHIN, ARJMAND, SAREH, & MOTA, ALI. (2012). EXPRESSION AND CHARACTERIZATION OF BACTERIAL ORGANOPHOSPHORUS HYDROLASE IN PICHIA PASTORIS WITH THE INTENT TO DEGRADE ORGANOPHOSPHATE NEUROTOXINS. PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES), 15(1), 61-72. SID. https://sid.ir/paper/80985/en

Vancouver: Copy

NAJAVAND SAEED, SAHEBGHADAM LOTFI ABBASS, MOHSENIFAR AFSHIN, ARJMAND SAREH, MOTA ALI. EXPRESSION AND CHARACTERIZATION OF BACTERIAL ORGANOPHOSPHORUS HYDROLASE IN PICHIA PASTORIS WITH THE INTENT TO DEGRADE ORGANOPHOSPHATE NEUROTOXINS. PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES)[Internet]. 2012;15(1):61-72. Available from: https://sid.ir/paper/80985/en

IEEE: Copy

SAEED NAJAVAND, ABBASS SAHEBGHADAM LOTFI, AFSHIN MOHSENIFAR, SAREH ARJMAND, and ALI MOTA, “EXPRESSION AND CHARACTERIZATION OF BACTERIAL ORGANOPHOSPHORUS HYDROLASE IN PICHIA PASTORIS WITH THE INTENT TO DEGRADE ORGANOPHOSPHATE NEUROTOXINS,” PATHOBIOLOGY RESEARCH (MODARES JOURNAL OF MEDICAL SCIENCES), vol. 15, no. 1, pp. 61–72, 2012, [Online]. Available: https://sid.ir/paper/80985/en

Related Journal Papers