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Publication
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| Research Title |
Purification and biochemical characterization of amylase enzyme from Puntioplites proctozysron |
| Date of Distribution |
5 October 2020 |
| Conference |
| Title of the Conference |
Power of Science to Achieve SDGs |
| Organiser |
The 46th International Congress on Science, Technology and Technology-based Innovation (STT46) |
| Conference Place |
Ramkhamhaeng University |
| Province/State |
Bangkok |
| Conference Date |
5 October 2020 |
| To |
7 October 2020 |
| Proceeding Paper |
| Volume |
46 |
| Issue |
1 |
| Page |
416-424 |
| Editors/edition/publisher |
The Science Society of Thailand Under the Patronage of His Majesty the King Faculty of Science, Ramkhamhaeng University |
| Abstract |
Amylase enzyme from Puntioplites proctozysron was purified and characterized. The enzyme was extracted from whole digestive tract. Purification was performed with the combination step of ammonium sulfate precipitation, anion exchange chromatography, and
size exclusion chromatography, respectively. The partially purified amylases were collected in three fractions including unbound fraction (UB), P1, and P2, which were then subjected for biochemical characterization. SDS-PAGE and zymogram showed the partially purified enzymes. All fractions exhibited the same optimum pH at 8.0 and different optimum temperatures at 60 ºC for UB and at 45 ºC for P1 and P2. The enzymes revealed stable at pH of 7.0-9.0 with residual activities more than 80% after both incubation of 1 h and 6 h. Upon incubation for 1 h, all three fractions exhibited high thermal stability at 29 ºC with increasing residual activity of 126.0% to 160.0%. Once increasing of incubation time to 6 h, the residual activities of enzymes reduced. However, P1 and P2 were still displayed high residual activities 94% and 95%, respectively. In addition, effects of metal ions and chemical reagents on enzyme activity showed that the amylase activities of all fractions were slightly enhanced in the presence of 2 mM Ca2+ ion and were strongly inhibited by Zn2+, SDS and EDTA, while monovalent cations of K+ and Na+ did not make any change of their activities. |
| Author |
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| Peer Review Status |
มีผู้ประเมินอิสระ |
| Level of Conference |
นานาชาติ |
| Type of Proceeding |
Full paper |
| Type of Presentation |
Oral |
| Part of thesis |
true |
| Presentation awarding |
false |
| Attach file |
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| Citation |
0
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Journal Publication
ไทย