Engineering of E. coli for increased production of L-lactic acid

An over-expressed L-ldh gene derivative of Escherichia coli BAD-ldh was developed. L-ldh gene from Enterococcus facelis KK1 consisted of an open reading frame of 954 bp encoding 316 amino acids. L-ldh gene was cloned into pBAD vector and transformed into E.coli SZ85 by electroporation. SDS-page and...

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Main Authors: Tengku Zainal Mulok, Tengku Elida, Chong, Mei Ling, Shirai, Yoshihito, Abdul Rahim, Raha, Hassan, Mohd Ali
Format: Article
Language:English
Published: Academic Journals 2009
Online Access:http://psasir.upm.edu.my/id/eprint/14503/1/14503.pdf
http://psasir.upm.edu.my/id/eprint/14503/
http://www.academicjournals.org/journal/AJB/article-abstract/EACCE0F9284
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Institution: Universiti Putra Malaysia
Language: English
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spelling my.upm.eprints.145032016-05-03T11:13:48Z http://psasir.upm.edu.my/id/eprint/14503/ Engineering of E. coli for increased production of L-lactic acid Tengku Zainal Mulok, Tengku Elida Chong, Mei Ling Shirai, Yoshihito Abdul Rahim, Raha Hassan, Mohd Ali An over-expressed L-ldh gene derivative of Escherichia coli BAD-ldh was developed. L-ldh gene from Enterococcus facelis KK1 consisted of an open reading frame of 954 bp encoding 316 amino acids. L-ldh gene was cloned into pBAD vector and transformed into E.coli SZ85 by electroporation. SDS-page and western blotting method confirmed the presence of recombinant L-LDH enzyme with the approximate size of 40kD. The activity of L-lactate dehydrogenase was achieved at 170 U ml¯¹. E.coli BAD85 was found to produce 0.62 g l¯¹ of lactic acid from 1 g 1¯¹ of fructose in 24 h. L-ldh gene from was successfully transformed into E.coli SZ85 with the maximum production of L-lactic acid at 0.62 g l¯¹. Academic Journals 2009 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/14503/1/14503.pdf Tengku Zainal Mulok, Tengku Elida and Chong, Mei Ling and Shirai, Yoshihito and Abdul Rahim, Raha and Hassan, Mohd Ali (2009) Engineering of E. coli for increased production of L-lactic acid. African Journal of Biotechnology, 8 (18). art. no. EACCE0F9284. pp. 4597-4603. ISSN 1684–5315 http://www.academicjournals.org/journal/AJB/article-abstract/EACCE0F9284
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
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language English
description An over-expressed L-ldh gene derivative of Escherichia coli BAD-ldh was developed. L-ldh gene from Enterococcus facelis KK1 consisted of an open reading frame of 954 bp encoding 316 amino acids. L-ldh gene was cloned into pBAD vector and transformed into E.coli SZ85 by electroporation. SDS-page and western blotting method confirmed the presence of recombinant L-LDH enzyme with the approximate size of 40kD. The activity of L-lactate dehydrogenase was achieved at 170 U ml¯¹. E.coli BAD85 was found to produce 0.62 g l¯¹ of lactic acid from 1 g 1¯¹ of fructose in 24 h. L-ldh gene from was successfully transformed into E.coli SZ85 with the maximum production of L-lactic acid at 0.62 g l¯¹.
format Article
author Tengku Zainal Mulok, Tengku Elida
Chong, Mei Ling
Shirai, Yoshihito
Abdul Rahim, Raha
Hassan, Mohd Ali
spellingShingle Tengku Zainal Mulok, Tengku Elida
Chong, Mei Ling
Shirai, Yoshihito
Abdul Rahim, Raha
Hassan, Mohd Ali
Engineering of E. coli for increased production of L-lactic acid
author_facet Tengku Zainal Mulok, Tengku Elida
Chong, Mei Ling
Shirai, Yoshihito
Abdul Rahim, Raha
Hassan, Mohd Ali
author_sort Tengku Zainal Mulok, Tengku Elida
title Engineering of E. coli for increased production of L-lactic acid
title_short Engineering of E. coli for increased production of L-lactic acid
title_full Engineering of E. coli for increased production of L-lactic acid
title_fullStr Engineering of E. coli for increased production of L-lactic acid
title_full_unstemmed Engineering of E. coli for increased production of L-lactic acid
title_sort engineering of e. coli for increased production of l-lactic acid
publisher Academic Journals
publishDate 2009
url http://psasir.upm.edu.my/id/eprint/14503/1/14503.pdf
http://psasir.upm.edu.my/id/eprint/14503/
http://www.academicjournals.org/journal/AJB/article-abstract/EACCE0F9284
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