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Characterization of Extracellular Penicilin G Acylase Produced by A New Local Strain of Bacillus subtilis BAC4

HAYATI Journal of Biosciences · Vol. 15 No. 2 (2009)

DOI
10.4308/hjb.15.2.71
ISSN
2086-4094, 1978-3019
Terbit
2009-12-03
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng

Abstrak

Penicillin G acylase (PGA) which catalyses penicillin G hydrolysis reaction is a key enzyme for the industrial production of penicilin G derivatives used in therapeutics. A new local strain of Bacillus subtilis BAC4 was found capable of producing extracellular PGA. However, characteristics of this extracellular PGA are not known. The goal of this research was to characterize the extracellular PGA produced by B. subtilis BAC4. Enzyme production was carried out by batch fermentation, followed by enzyme purification and characterization of the PGA. The PGA activity was determined by the Kornfeld method, with optimal activity for hydrolysing penicillin G observed at 43 oC and pH 8.5. The activation energy of penicillin G hydrolysis by the PGA of B. subtilis BAC4 was determined as 4.9 kcal.mol-1 and Vmax and Km values were found to be 0.7 µmole.min-1.mg-1 and 3.5 mM respectively. PGA catalytic activity was competitively inhibited by phenylacetic acid with an inhibition constant, Ki(PAA), of 347.2 mM. It was concluded that the extracellular PGA of B. subtilis BAC4 can hydrolyse penicillin G efficiently. Key words: PGA, extracellular, Bacillus, local

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  • Bandung Institute of Technology
  • State University of Semarang
  • Yogyakarta State University
  • 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
N. M. SurdiaBandung Institute of Technology4
Cynthia Linaya RadimanBandung Institute of Technology3
Rukman HertadiBandung Institute of Technology2
Sri Mulyani Endang SusilowatiState University of Semarang2
Eli RohaetiYogyakarta State University2
Bambang AriwahjoediBandung Institute of Technology2
Zuhdina SabiqohBandung Institute of Technology1
Ridani Rino AnggoroBandung Institute of Technology1
Ni Putu YuliastriBandung Institute of Technology1
Idris IdrisUniversitas Islam Negeri Sultan Maulana Hasanuddin Banten1
Wiyanto WiyantoState University of Semarang1
Woro SumarniState University of Semarang1
Sudarmin SudarminState University of Semarang1
Hartono HartonoState University of Semarang1
Sugito SugitoState University of Semarang1
Hartono HartonoState University of Semarang1
Sugito SugitoYogyakarta State University1
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
Buchari BuchariAfiliasi tidak diketahui1
Yana Maolana SyahBandung Institute of Technology1
Deana WahyuningrumBandung Institute of Technology1
Marlina MarlinaAfiliasi tidak diketahui1
Bunbun BundjaliBandung Institute of Technology1

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Sumber metadata: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/hayati/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">Characterization of Extracellular Penicilin G Acylase Produced by A New Local Strain of Bacillus subtilis BAC4</dc:title>
	<dc:creator xml:lang="en">SUPARTONO, SUPARTONO</dc:creator>
	<dc:creator xml:lang="en">RATNANINGSIH, ENNY</dc:creator>
	<dc:creator xml:lang="en">ACHMAD, SADIJAH</dc:creator>
	<dc:creator xml:lang="en">LIANG, OEI BAN</dc:creator>
	<dc:description xml:lang="en">Penicillin G acylase (PGA) which catalyses penicillin G hydrolysis reaction is a key enzyme for the industrial production of penicilin G derivatives used in therapeutics. A new local strain of Bacillus subtilis BAC4 was found capable of producing extracellular PGA. However, characteristics of this extracellular PGA are not known. The goal of this research was to characterize the extracellular PGA produced by B. subtilis BAC4. Enzyme production was carried out by batch fermentation, followed by enzyme purification and characterization of the PGA. The PGA activity was determined by the Kornfeld method, with optimal activity for hydrolysing penicillin G observed at 43 oC and pH 8.5. The activation energy of penicillin G hydrolysis by the PGA of B. subtilis BAC4 was determined as 4.9 kcal.mol-1 and Vmax and Km values were found to be 0.7 µmole.min-1.mg-1 and 3.5 mM respectively. PGA catalytic activity was competitively inhibited by phenylacetic acid with an inhibition constant, Ki(PAA) , of 347.2 mM. It was concluded that the extracellular PGA of  B. subtilis BAC4 can hydrolyse penicillin G efficiently. Key words: PGA, extracellular, Bacillus, local </dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2009-12-03</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">Peer-reviewed Article</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>http://journal.ipb.ac.id/hayati/article/view/273</dc:identifier>
	<dc:identifier>10.4308/hjb.15.2.71</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 15 No. 2 (2008): June 2008; 71</dc:source>
	<dc:source>2086-4094</dc:source>
	<dc:source>1978-3019</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>http://journal.ipb.ac.id/hayati/article/view/273/138</dc:relation>
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