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Fractionation and Characterization of Tannin Acyl Hydrolase from Aspergillus niger

HAYATI Journal of Biosciences · Vol. 16 No. 3 (2010)

DOI
10.4308/hjb.16.3.95
ISSN
2086-4094, 1978-3019
Terbit
2010-01-06
Penerbit
Bogor Agricultural University, Indonesia
Bahasa
eng

Abstrak

We previously produced tannin acyl hydrolase (tannase) from Aspergillus niger isolated from cacao pod. In the present study the enzyme was subjected to fractionation by ammonium sulphate followed by dialysis process. The saturation level of ammonium sulphate used was 30-80% where the best enzyme activity was obtained at the saturation level of 60%. Compared to that of crude enzyme, specific activity of tannase after dialysis was four folds. Characterization results showed that optimum activity was at 35-50 oC and pH 6. Tannase was activated by K+ and Na+ at concentration of 0.01 and 0.05 M respectively. Mg2+ was found activate tannase only at 0.01 M. Addition of metal ions like Zn2+, Cu2+, Ca2+, Mn2+ and Fe2+ inhibited the enzyme activity. Kinetics analysis of various substrates tested showed that the Km value of tannic acid and gallotannin was 0.401 and 6.611 mM respectively. Vmax value of tannic acid was 10.804 U/ml and of gallotannin was 12.406 U/ml. Based on Michaelis-Menten constant (Km), the tannase obtained in the present study was more active in hydrolysing depside bonds rather than ester bonds. Key words: tannase, fermentation, fractionation, characterization, Aspergillus niger

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  • IPB University
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  • University of Mataram
  • Universitas Jambi
  • University of Indonesia
  • Universitas Halu Oleo
  • Jenderal Soedirman University
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Rekan penulisOrganisasiArtikel bersama
Muhaimin MuhaiminUniversitas Jambi2
Andita Fitri Mutiara RizkiNational Research and Innovation Agency2
Wihda Aisarul AzmiNational Research and Innovation Agency2
Melva LouisaUniversity of Indonesia2
Josephine Elizabeth SiregarNational Research and Innovation Agency2
. SuryaniUniversitas Halu Oleo2
Akhmad Endang Zainal HasanIPB University1
Dhani Luthfi RamadhaniIPB University1
KUSWANDI KUSWANDIAfiliasi tidak diketahui1
Amin FatoniJenderal Soedirman University1
AHMAD ENDANG ZAINAL HASANIPB University1
Dimas AndriantoIPB University1
Latifah Kosim DarusmanIPB University1
Sulistiyani SulistiyaniIPB University1
HARTUTIK EKA SUSANTIIPB University1
Laksmi AmbarsariIPB University1
Apon Zaenal MustopaNational Research and Innovation Agency1
Sogandi SogandiUniversitas 17 Agustus 1945 Jakarta1
Waras NurcholisIPB University1
Siahaan RafaelIPB University1
Eka Rahmat HidayatIPB University1
Yanuar Jarwadi PurwantoIPB University1

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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">Fractionation and Characterization of Tannin Acyl Hydrolase from Aspergillus niger</dc:title>
	<dc:creator xml:lang="en">SANI ANWAR, YUNITA ARIAN</dc:creator>
	<dc:creator xml:lang="en">ARTIKA, I MADE</dc:creator>
	<dc:creator xml:lang="en">DANURI, HASIM</dc:creator>
	<dc:description xml:lang="en">We previously produced tannin acyl hydrolase (tannase) from Aspergillus niger isolated from cacao pod. In the present study the enzyme was subjected to fractionation by ammonium sulphate followed by dialysis process. The saturation level of ammonium sulphate used was 30-80% where the best enzyme activity was obtained at the saturation level of 60%. Compared to that of crude enzyme, specific activity of tannase after dialysis was four folds. Characterization results showed that optimum activity was at 35-50 oC and pH 6. Tannase was activated by K+ and Na+ at concentration of 0.01 and 0.05 M respectively.  Mg2+ was found activate tannase only at 0.01 M.  Addition of metal ions like Zn2+, Cu2+, Ca2+, Mn2+ and Fe2+ inhibited the enzyme activity. Kinetics analysis of various substrates tested showed that the Km value of tannic acid and gallotannin was 0.401 and 6.611 mM respectively. Vmax value of tannic acid was 10.804 U/ml and of gallotannin was 12.406 U/ml. Based on Michaelis-Menten constant (Km), the tannase obtained in the present study was more active in hydrolysing depside bonds rather than ester bonds. Key words: tannase, fermentation, fractionation, characterization, Aspergillus niger </dc:description>
	<dc:publisher xml:lang="en">Bogor Agricultural University, Indonesia</dc:publisher>
	<dc:date>2010-01-06</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/279</dc:identifier>
	<dc:identifier>10.4308/hjb.16.3.95</dc:identifier>
	<dc:source xml:lang="en">HAYATI Journal of Biosciences; Vol. 16 No. 3 (2009): September 2009; 95</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/279/144</dc:relation>
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