Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad

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.

SALEHI M.; AGHAMAALI M.R.; HASSAN SAJEDI R.; ASGHARI S.M.; Jorjani I.

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

Journal Paper

Paper Information

Journal: JOURNAL OF BIOTECHNOLOGY Year:2019 | Volume:10 | Issue:1 Page(s): 53-60

Download Full-Text

Persian Verion

View:

798

Download:

Cites:

Information Journal Paper

Title

Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad

Author(s)

Keywords

Aspartic Acid ProteaseQ1

PaneerbadQ1

Metal IonsQ1

Abstract

The fruit of Paneerbad has a lot of acidic proteases and its extract has been used in cheese manufacturing. However, there are few studies about purification and characterization of this enzyme. Following conditions must be satisfied for the enzyme to be used in industry: 1-stability of enzymes against Metal Ions and 2-Ability to sustain proper function and stability in the absence of metal ion. Accordingly, in this investigation, the effect of various ions at different concentrations on activity, stability and somewhat on structural properties of the purified protease were studied. Based on the results, it was shown that the enzyme was relatively stable against NaCl and CaCl2, but by increment of these salts, stability and activity of enzyme was decreased. Also, the enzyme was stable against low concentration of various Metal Ions and only Hg2+ significantly reduces enzyme stability and activity. By studying the role of Ca2+ on thermostability of enzyme, it was found that ca2+ didn’ t have any role in thermal stability of enzyme at 67˚ C. Likewise, by observing the effect of Metal Ions on intrinsic fluorescence of enzyme it was cleared that all tested ions increased intensity of emission and caused to shift maximum wave length toward lower wave length. In all, results of these study showed that the purified enzyme from paneer bad is very stable against various Metal Ions especially heavy metals and therefor it is favorable for industrial application.

Cites

No record.

References

No record.

Cite

APA: Copy

SALEHI, M., AGHAMAALI, M.R., HASSAN SAJEDI, R., ASGHARI, S.M., & Jorjani, I.. (2019). Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad. JOURNAL OF BIOTECHNOLOGY, 10(1 ), 53-60. SID. https://sid.ir/paper/231237/en

Vancouver: Copy

SALEHI M., AGHAMAALI M.R., HASSAN SAJEDI R., ASGHARI S.M., Jorjani I.. Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad. JOURNAL OF BIOTECHNOLOGY[Internet]. 2019;10(1 ):53-60. Available from: https://sid.ir/paper/231237/en

IEEE: Copy

M. SALEHI, M.R. AGHAMAALI, R. HASSAN SAJEDI, S.M. ASGHARI, and I. Jorjani, “Effect of Metal Ions on Activity, Stability, and Structure of Purified Aspartic Protease from Paneerbad,” JOURNAL OF BIOTECHNOLOGY, vol. 10, no. 1 , pp. 53–60, 2019, [Online]. Available: https://sid.ir/paper/231237/en

Related Journal Papers