Effect of Amylose Content on Corn Starch Modification by Thermus aquaticus 4-α-Glucanotransferase

Corn starches with different amylose contents were enzymatically modified using Thermus aquaticus 4-α-glucanotransferase (TAαGTase). Upon the enzyme treatment, the chain-length distributions of isoamylolytically debranched products became broader [degree of polymerization (DP): 3-40] than those of u...

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Published inJournal of microbiology and biotechnology Vol. 19; no. 10; pp. 1201 - 1205
Main Authors Cho, K.H., Sejong University, Seoul, Republic of Korea, Auh, J.H., Chung-Ang University, Ansung, Republic of Korea, Kim, J.H., Sejong University, Seoul, Republic of Korea, Ryu, J.H., Sejong University, Seoul, Republic of Korea, Park, K.H., University of Incheon, Incheon, Republic of Korea, Park, C.S., Kyung Hee University, Yongin, Republic of Korea, Yoo, S.H., Sejong University, Seoul, Republic of Korea
Format Journal Article
LanguageEnglish
Published Seoul Korean Society for Applied Microbiology 01.10.2009
한국미생물·생명공학회
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ISSN1017-7825
DOI10.4014/jmb.0905.05048

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Summary:Corn starches with different amylose contents were enzymatically modified using Thermus aquaticus 4-α-glucanotransferase (TAαGTase). Upon the enzyme treatment, the chain-length distributions of isoamylolytically debranched products became broader [degree of polymerization (DP): 3-40] than those of untreated corn starches. In addition, a variety of cycloamyloses (CAs) with different sizes were formed by the glucanotransfer activity of TAαGTase. CAs with DP 5-40 were detectable in all of the TAαGTase-treated corn starches. From the results of high-performance anion-exchange chromatography and high-performance size-exclusion chromatography analyses, it was suggested that the amount of CAs produced by the enzyme treatment increased as the amylose content of the starches increased. Thus, we concluded that the extent of modification of Starch molecules was enhanced in proportion to amylose content by the transfer activity of TAαGTase. This finding could be useful for developing an efficient process of CA production using this enzyme.
Bibliography:A50
2010002424
G704-000169.2009.19.10.023
ISSN:1017-7825
DOI:10.4014/jmb.0905.05048