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Expression of haloacid dehalogenase gene and its molecular protein characterization from Klebsiella pneumoniae ITB1

Indonesian Journal of Biotechnology · Vol. 22 No. 1 (2017) · hlm. 1–5

DOI
10.22146/ijbiotech.26004
ISSN
2089-2241, 0853-8654
Terbit
2017-06-01
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

Organohalogen compounds are widely used industrially and agriculturally, as well as in households as flame retardants and refrigerants. However, these compounds can become significant pollutants through their accidental or deliberate release into the environment in large quantities. Dehalogenase is an enzyme with the potential to be used in the removal of organohalogen contaminants. A previous study successfully subcloned a 690 bp of haloacid dehalogenase gene (hakp1) from Klebsiella pneumoniae ITB1 into a pET-30a(+) expression system to achieve high enzyme productivity. IPTG was used as an inducer to express a pET-hakp1 recombinant clone in Escherichia coli BL21 (DE3). The molecular mass of the haloacid dehalogenase Hakp1 protein was 30 kDa as determined by SDS-PAGE. Zymogram analysis showed that this recombinant protein has dehalogenase activity as shown by the formation of AgCl white precipitate. A quantitative assay of haloacid dehalogenase Hakp1 gave a specific activity of 84.29 U/mg with the optimum temperature of 40°C at pH 9. Predicted three-dimensional structure of Hakp1 showed α/β motif folding which comprised of cap and core domain. The predicted active sites of Hakp1 were Asp8, Glu10, Leu22, Phe23, Trp90, Ser125, Ser126, Lys159, and Asp184 with Asp8, Glu10, Ser126, and Lys159 act as binding residue. This recombinant haloacid dehalogenase clone provides an alternative agent for effective bioremediation of organohalogen pollutants.

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22 penulis · 56 tautan kepenulisan bersama · 23 lintas organisasi

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  • Bandung Institute of Technology
  • Yogyakarta State University
  • State University of Semarang
  • Universitas Islam Negeri Sultan Maulana Hasanuddin Banten
  • Indonesian Institute of Sciences
  • Universitas Jenderal Achmad Yani
  • University of Brawijaya
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Rekan penulisOrganisasiArtikel bersama
Rukman HertadiBandung Institute of Technology2
Eli RohaetiYogyakarta State University2
Cynthia Linaya RadimanBandung Institute of Technology2
N. M. SurdiaBandung Institute of Technology2
Supartono SupartonoState University of Semarang1
Sadijah AchmadBandung Institute of Technology1
Oei Ban LiangBandung Institute of Technology1
Zuhdina SabiqohBandung Institute of Technology1
Ni Putu YuliastriBandung Institute of Technology1
Idris IdrisUniversitas Islam Negeri Sultan Maulana Hasanuddin Banten1
Idris IdrisIndonesian Institute of Sciences1
Rachmad AdeBandung Institute of Technology1
Rindia M. PutriBandung Institute of Technology1
K. KhoiruddinBandung Institute of Technology1
I Gede WentenBandung Institute of Technology1
Putu Teta Prihartini AryantiUniversitas Jenderal Achmad Yani1
Anita Kusuma WardaniBandung Institute of Technology1
Grandprix T.M. KadjaBandung Institute of Technology1
Nurul Faiqotul HimmaUniversity of Brawijaya1
Nicholaus PrasetyaBandung Institute of Technology1

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Sumber metadata: OAI-PMH (metadata jurnal) https://jurnal.ugm.ac.id/ijbiotech/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (oai_dc) 
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	<dc:title xml:lang="en-US">Expression of haloacid dehalogenase gene and its molecular protein characterization from Klebsiella pneumoniae ITB1</dc:title>
	<dc:creator>Anggoro, Ridani Rino</dc:creator>
	<dc:creator>Ratnaningsih, Enny</dc:creator>
	<dc:subject xml:lang="en-US">Haloacid dehalogenase; Klebsiella pneumoniae ITB1; organohalogen</dc:subject>
	<dc:description xml:lang="en-US">Organohalogen compounds are widely used industrially and agriculturally, as well as in households as flame retardants and refrigerants. However, these compounds can become significant pollutants through their accidental or deliberate release into the environment in large quantities. Dehalogenase is an enzyme with the potential to be used in the removal of organohalogen contaminants. A previous study successfully subcloned a 690 bp of haloacid dehalogenase gene (hakp1) from Klebsiella pneumoniae ITB1 into a pET-30a(+) expression system to achieve high enzyme productivity. IPTG was used as an inducer to express a pET-hakp1 recombinant clone in Escherichia coli BL21 (DE3). The molecular mass of the haloacid dehalogenase Hakp1 protein was 30 kDa as determined by SDS-PAGE. Zymogram analysis showed that this recombinant protein has dehalogenase activity as shown by the formation of AgCl white precipitate. A quantitative assay of haloacid dehalogenase Hakp1 gave a specific activity of 84.29 U/mg with the optimum temperature of 40°C at pH 9. Predicted three-dimensional structure of Hakp1 showed α/β motif folding which comprised of cap and core domain. The predicted active sites of Hakp1 were Asp8, Glu10, Leu22, Phe23, Trp90, Ser125, Ser126, Lys159, and Asp184 with Asp8, Glu10, Ser126, and Lys159 act as binding residue. This recombinant haloacid dehalogenase clone provides an alternative agent for effective bioremediation of organohalogen pollutants.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US">Lembaga Pengelola Dana Pendidikan (LPDP) Indonesia</dc:contributor>
	<dc:date>2017-06-01</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:type xml:lang="en-US">Original Research Articles</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.ugm.ac.id/ijbiotech/article/view/26004</dc:identifier>
	<dc:identifier>10.22146/ijbiotech.26004</dc:identifier>
	<dc:source xml:lang="en-US">Indonesian Journal of Biotechnology; Vol 22, No 1 (2017); 1-5</dc:source>
	<dc:source>2089-2241</dc:source>
	<dc:source>0853-8654</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.ugm.ac.id/ijbiotech/article/view/26004/19513</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2017 The Author(s)</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
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