Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/56845
Title: Partial purification and comparison of precipitation techniques of pyruvate decarboxylase enzyme
Authors: Julaluk Tangtua
Charin Techapun
Ronachai Pratanaphon
Ampin Kuntiya
Vorapat Sanguanchaipaiwong
Thanongsak Chaiyaso
Prasert Hanmoungjai
Phisit Seesuriyachan
Nopphorn Leksawasdi
Noppol Leksawasdi
Authors: Julaluk Tangtua
Charin Techapun
Ronachai Pratanaphon
Ampin Kuntiya
Vorapat Sanguanchaipaiwong
Thanongsak Chaiyaso
Prasert Hanmoungjai
Phisit Seesuriyachan
Nopphorn Leksawasdi
Noppol Leksawasdi
Keywords: Biochemistry, Genetics and Molecular Biology;Chemistry;Materials Science;Mathematics;Physics and Astronomy
Issue Date: 1-Jan-2017
Abstract: © 2017, Chiang Mai University. All rights reserved. The intracellular pyruvate decarboxylase enzyme (PDC, EC 4.1.1.1) extract from Candida tropicalis TISTR 5350 was compared by two different purification methods using ammonium sulphate and acetone precipitation. The total volumetric PDC activity and percentage recovery (yield) of precipitated PDC based on 50% (v/v) cold acetone were significantly higher (1.13 ± 0.02 U/ml and 98.27 ± 2.98 %, respectively) than any other concentration levels of acetone used. Furthermore, all concentration levels of cold acetone also yielded a much higher specific PDC activity than the precipitate obtained using the 40 to 60% (w/v) ammonium sulphate saturation (0.75 ± 0.08 U/mg protein). The precipitated enzyme in buffer solutions from the 50% (v/v) acetone was subsequently freeze dried. Freeze drying of the precipitated PDC by cold acetone resulted in the specific PDC activity of 1.57 ± 0.02 U/mg protein and differed statistically (p ≤ 0.05) from the crude enzyme extract (control).
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85010739408&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/56845
ISSN: 01252526
Appears in Collections:CMUL: Journal Articles

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