THE STUDY ON THE INTERACTION OF Α - AMYLASE FROM B. SUBTILLS AND SODIUM DODECYL SULPHATE

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.

SHAREGHI B.

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

Journal Paper

Paper Information

Journal: SHAHID CHAMRAN UNIVERSITY JOURNAL OF SCIENCE Year:2006 | Volume:NEW SERIES | Issue:15 (SECTION B) Page(s): 1-17

Download Full-Text

Persian Verion

View:

1,626

Download:

Cites:

Information Journal Paper

Title

THE STUDY ON THE INTERACTION OF Α - AMYLASE FROM B. SUBTILLS AND SODIUM DODECYL SULPHATE

Author(s)

SHAREGHI B. | Issue Writer Certificate

Keywords

Α-AMYLASEQ3

STABILITYQ3

THERMODYNAMICQ3

KINETICQ3

Abstract

The interaction of sodium n-dodecyl sulphate and thermophilic α -Amylase from b.subtilis has been investigated employing UV spectrophotometry and KINETICs measurments.Spectroscopic measurements were implemented at λ=180nm over the temperature range (20- 105°C) in 0.02M sodium phosphate buffer pH=6.9. KINETICs measurements were also used at different temperature and over the pH range (2-13). It has been observed that 1), enzyme shows striking STABILITY, 2), the interaction of SDS (as a potent denaturant) with α – Amylase has no affect on the STABILITY of the enzyme in a temperature less than 90°C, 3), in the presence of SDS THERMODYNAMICs parameters, ΔH°m, Δs°m, ΔCP decrease more than 90°C and 4), KINETICs measurements at 95°C show small decrease on the activity of α -Amylase in the presence of SDS.

Cites

FACIES AND DEPOSITIONAL ENVIRONMENTS OF THE QOM FORMATION IN BAND-E-AMIR SECTION IN NORTHWEST OF SAVEH

References

No record.

Cite

APA: Copy

SHAREGHI, B.. (2006). THE STUDY ON THE INTERACTION OF Α - AMYLASE FROM B. SUBTILLS AND SODIUM DODECYL SULPHATE. SHAHID CHAMRAN UNIVERSITY JOURNAL OF SCIENCE, NEW SERIES(15 (SECTION B)), 1-17. SID. https://sid.ir/paper/57994/en

Vancouver: Copy

SHAREGHI B.. THE STUDY ON THE INTERACTION OF Α - AMYLASE FROM B. SUBTILLS AND SODIUM DODECYL SULPHATE. SHAHID CHAMRAN UNIVERSITY JOURNAL OF SCIENCE[Internet]. 2006;NEW SERIES(15 (SECTION B)):1-17. Available from: https://sid.ir/paper/57994/en

IEEE: Copy

B. SHAREGHI, “THE STUDY ON THE INTERACTION OF Α - AMYLASE FROM B. SUBTILLS AND SODIUM DODECYL SULPHATE,” SHAHID CHAMRAN UNIVERSITY JOURNAL OF SCIENCE, vol. NEW SERIES, no. 15 (SECTION B), pp. 1–17, 2006, [Online]. Available: https://sid.ir/paper/57994/en

Related Journal Papers