Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis

Objectives: Cyclodextrin glucanotransferase (CGTase) is a multifunctional industrial enzyme, which undergoes cyclization reaction to converts starch into Cyclodextrin (CD). Due to their potential properties, CDs had been discovered to have numerous application in food industries, pharmaceutical, agr...

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Main Authors: N., Jamil, Rohaida, Che Man, Shalyda, Md Shaarani, Siti Zubaidah, Sulaiman, Siti Kholijah, Abdul Mudalip, Zatul Iffah, Mohd Arshad
Format: Article
Language:English
Published: Informatics Publishing Limited 2017
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Online Access:http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/1/fkksa-2017-rohaida-Characterization%20of%20%CE%B1-Cyclodextrin.pdf
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spelling ump-174682017-08-16T03:00:28Z http://umpir.ump.edu.my/id/eprint/17468/ Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis N., Jamil Rohaida, Che Man Shalyda, Md Shaarani Siti Zubaidah, Sulaiman Siti Kholijah, Abdul Mudalip Zatul Iffah, Mohd Arshad TP Chemical technology Objectives: Cyclodextrin glucanotransferase (CGTase) is a multifunctional industrial enzyme, which undergoes cyclization reaction to converts starch into Cyclodextrin (CD). Due to their potential properties, CDs had been discovered to have numerous application in food industries, pharmaceutical, agriculture and also environmental engineering. To improve the production of cyclodextrin (CD) in the future, characterization of α-CGTase on the effect of operating conditions was investigated. Methods/Statistical Analysis: The α-CGTase from Bacillus licheniformis was characterized by examining their cyclization activity. The enzymatic activity of the enzyme towards the temperature and pH was determined by methyl orange method. Findings: The enzyme was estimated to be 70 kDa by the gel electrophoresis. The cyclization activity of α-CGTase was highest at a temperature of 40°C and pH 6.0. The α-CGTase enzyme was able to extend its thermostability up to 60°C with pH stability between pH 6.0 and pH 8.0. Application/Improvements: High production of CD is expected to obtain by using the optimal conditions which in turn may be beneficial for the industrial purpose. Informatics Publishing Limited 2017 Article PeerReviewed application/pdf en cc_by http://umpir.ump.edu.my/id/eprint/17468/1/fkksa-2017-rohaida-Characterization%20of%20%CE%B1-Cyclodextrin.pdf N., Jamil and Rohaida, Che Man and Shalyda, Md Shaarani and Siti Zubaidah, Sulaiman and Siti Kholijah, Abdul Mudalip and Zatul Iffah, Mohd Arshad (2017) Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis. Indian Journal of Science and Technology, 10 (7). pp. 1-5. ISSN 0974-6846 (Print); 0974-5645 (Online) http://www.indjst.org/index.php/indjst/article/view/111220 DOI: 10.17485/ijst/2017/v10i7/111220
repository_type Digital Repository
institution_category Local University
institution Universiti Malaysia Pahang
building UMP Institutional Repository
collection Online Access
language English
topic TP Chemical technology
spellingShingle TP Chemical technology
N., Jamil
Rohaida, Che Man
Shalyda, Md Shaarani
Siti Zubaidah, Sulaiman
Siti Kholijah, Abdul Mudalip
Zatul Iffah, Mohd Arshad
Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
description Objectives: Cyclodextrin glucanotransferase (CGTase) is a multifunctional industrial enzyme, which undergoes cyclization reaction to converts starch into Cyclodextrin (CD). Due to their potential properties, CDs had been discovered to have numerous application in food industries, pharmaceutical, agriculture and also environmental engineering. To improve the production of cyclodextrin (CD) in the future, characterization of α-CGTase on the effect of operating conditions was investigated. Methods/Statistical Analysis: The α-CGTase from Bacillus licheniformis was characterized by examining their cyclization activity. The enzymatic activity of the enzyme towards the temperature and pH was determined by methyl orange method. Findings: The enzyme was estimated to be 70 kDa by the gel electrophoresis. The cyclization activity of α-CGTase was highest at a temperature of 40°C and pH 6.0. The α-CGTase enzyme was able to extend its thermostability up to 60°C with pH stability between pH 6.0 and pH 8.0. Application/Improvements: High production of CD is expected to obtain by using the optimal conditions which in turn may be beneficial for the industrial purpose.
format Article
author N., Jamil
Rohaida, Che Man
Shalyda, Md Shaarani
Siti Zubaidah, Sulaiman
Siti Kholijah, Abdul Mudalip
Zatul Iffah, Mohd Arshad
author_facet N., Jamil
Rohaida, Che Man
Shalyda, Md Shaarani
Siti Zubaidah, Sulaiman
Siti Kholijah, Abdul Mudalip
Zatul Iffah, Mohd Arshad
author_sort N., Jamil
title Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
title_short Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
title_full Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
title_fullStr Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
title_full_unstemmed Characterization of α-Cyclodextrin Glucanotransferase from Bacillus licheniformis
title_sort characterization of α-cyclodextrin glucanotransferase from bacillus licheniformis
publisher Informatics Publishing Limited
publishDate 2017
url http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/
http://umpir.ump.edu.my/id/eprint/17468/1/fkksa-2017-rohaida-Characterization%20of%20%CE%B1-Cyclodextrin.pdf
first_indexed 2023-09-18T22:24:08Z
last_indexed 2023-09-18T22:24:08Z
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