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Biochemical properties of crude extracellular proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A

Indonesian Journal of Biotechnology · Vol. 21 No. 1 (2016) · hlm. 56–62

DOI
10.22146/ijbiotech.26705
ISSN
2089-2241, 0853-8654
Terbit
2016-06-01
Penerbit
Universitas Gadjah Mada
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

In this work, we have reported an enzymatic activity and biochemical properties of extracellular proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A. C. salexigens BKL5 and M. luteus 11A were previously isolated from Bledug Kuwu mud volcano and dietary industry wastewater treatment, respectively. Both bacterial strains were able to produce extracellular proteases, when grown on minimal agar medium supplemented with 1% of skim milk. Proteolytic indexes of C. salexigens BKL5 and M. luteus 11A were 2.5±0.14 and 2.9±0.42, respectively. Both extracellular proteases exhibited optimum enzymatic activity at pH 7, with specific activity of C. salexigens BKL5 was 13.3% higher than that of M. luteus 11A. Optimum temperature for enzymatic activity of both proteases was 45°C. Metal cofactor preferences assay showed that extracellular protease from C. salexigens BKL5 preferred Zn2+, meanwhile extracellular protease from M. luteus 11A mainly preferred Ca2+ ion. Metal cofactor preferences assay also suggested that crude extracellular protease from C. salexigens BKL5 was categorized as metalloprotease, meanwhile crude extracellular protease of M. luteus 11A was common neutral protease. The enzymatic stability assay against various salt concentrations showed that crude extracellular protease from C. salexigens BKL5 was more stable than that of M. luteus 11A.

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  • Universitas Gadjah Mada
  • Sebelas Maret University
  • Lampung University
  • Ministry of Marine Affairs and Fisheries
  • IPB University
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  • Organisasi berbeda
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Rekan penulisOrganisasiArtikel bersama
Donny WidiantoUniversitas Gadjah Mada5
Jaka WidadaUniversitas Gadjah Mada3
Chusnul HidayatUniversitas Gadjah Mada2
J. JasmanUniversitas Gadjah Mada2
Sebastian MarginoUniversitas Gadjah Mada2
Triwibowo YuwonoUniversitas Gadjah Mada2
Yohanna Anisa IndriyaniIPB University2
Heri HendrosatriyoUniversitas Gadjah Mada2
Siti Lusi Arum SariSebelas Maret University1
Triyanto TriyantoUniversitas Gadjah Mada1
Zuprizal ZuprizalUniversitas Gadjah Mada1
Akbar ArofatullahAfiliasi tidak diketahui1
Lucia Dhiantika WitasariUniversitas Gadjah Mada1
Dionysius Andang Arif WibawaUniversitas Gadjah Mada1
Pintaka KusumaningtyasUniversitas Gadjah Mada1
Dhani SuryawanUniversitas Gadjah Mada1
Rusdi EvizalLampung University1
Siti KabirunUniversitas Gadjah Mada1
Sri WedhastriUniversitas Gadjah Mada1
Dinar Mindrati FardhaniUniversitas Gadjah Mada1
Erni MartaniUniversitas Gadjah Mada1
Endang PamulatsihUniversitas Gadjah Mada1
Yudi KusnadiMinistry of Marine Affairs and Fisheries1
Listia PradaniUniversitas Gadjah Mada1
Adinda Fitri SalsabilaUniversitas Gadjah Mada1
Abidah TauchidUniversitas Gadjah Mada1

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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">Biochemical properties of crude extracellular proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A</dc:title>
	<dc:creator>Achmad, Ayu Ashari</dc:creator>
	<dc:creator>Rohman, M. Saifur</dc:creator>
	<dc:creator>Prijambada, Irfan D.</dc:creator>
	<dc:subject xml:lang="en-US">extracellular protease; Chromohalobacter salexigens BKL5; Micrococcus luteus 11A; neutral protease; metalloprotease</dc:subject>
	<dc:description xml:lang="en-US">In this work, we have reported an enzymatic activity and biochemical properties of extracellular proteases from Chromohalobacter salexigens BKL5 and Micrococcus luteus 11A. C. salexigens BKL5 and M. luteus 11A were previously isolated from Bledug Kuwu mud volcano and dietary industry wastewater treatment, respectively. Both bacterial strains were able to produce extracellular proteases, when grown on minimal agar medium supplemented with 1% of skim milk. Proteolytic indexes of C. salexigens BKL5 and M. luteus 11A were 2.5±0.14 and 2.9±0.42, respectively. Both extracellular proteases exhibited optimum enzymatic activity at pH 7, with specific activity of C. salexigens BKL5 was 13.3% higher than that of M. luteus 11A. Optimum temperature for enzymatic activity of both proteases was 45°C. Metal cofactor preferences assay showed that extracellular protease from C. salexigens BKL5 preferred Zn2+, meanwhile extracellular protease from M. luteus 11A mainly preferred Ca2+ ion. Metal cofactor preferences assay also suggested that crude extracellular protease from C. salexigens BKL5 was categorized as metalloprotease, meanwhile crude extracellular protease of M. luteus 11A was common neutral protease. The enzymatic stability assay against various salt concentrations showed that crude extracellular protease from C. salexigens BKL5 was more stable than that of M. luteus 11A.</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Gadjah Mada</dc:publisher>
	<dc:contributor xml:lang="en-US"></dc:contributor>
	<dc:date>2016-06-01</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/26705</dc:identifier>
	<dc:identifier>10.22146/ijbiotech.26705</dc:identifier>
	<dc:source xml:lang="en-US">Indonesian Journal of Biotechnology; Vol 21, No 1 (2016); 56-62</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/26705/16535</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2016 The Author(s)</dc:rights>
	<dc:rights xml:lang="en-US">http://creativecommons.org/licenses/by-sa/4.0</dc:rights>
</oai_dc:dc>