Melola Discovery

← Melola Discovery

Journal SINTA 1

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
Published
2010-01-06
Publisher
Bogor Agricultural University, Indonesia
Language
eng

Abstract

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

Collaboration network of the authors

31 authors · 79 co-authorship links

Hover or tap a name to highlight its co-authors. Double-click to open the author's page.

  • Universitas Islam Negeri Antasari Banjarmasin
  • Universitas Halu Oleo
  • Affiliation unknown
  • Different organisations
  • Same organisation
  • Affiliation unknown
  • Thicker line = more joint articles · bigger circle = more articles
Show as table
Co-authorOrganisationJoint articles
Josephine Elizabeth SiregarAffiliation unknown3
Muhaimin MuhaiminUniversitas Islam Negeri Antasari Banjarmasin2
Andita Fitri Mutiara RizkiAffiliation unknown2
Wihda Aisarul AzmiAffiliation unknown2
Melva LouisaAffiliation unknown2
. SuryaniUniversitas Halu Oleo2
Akhmad Endang Zainal HasanAffiliation unknown1
Dhani Luthfi RamadhaniAffiliation unknown1
AMIN FATONIAffiliation unknown1
AHMAD ENDANG ZAINAL HASANAffiliation unknown1
KUSWANDI KUSWANDIAffiliation unknown1
Dimas AndriantoAffiliation unknown1
Sulistiyani SulistiyaniAffiliation unknown1
LATIFAH KOSIM DARUSMANAffiliation unknown1
Laksmi AmbarsariAffiliation unknown1
HARTUTIK EKA SUSANTIAffiliation unknown1
Apon Zaenal MustopaAffiliation unknown1
Sogandi SogandiAffiliation unknown1
Tri Rini NuringtyasAffiliation unknown1
Naufal AbiyyuAffiliation unknown1
Alfia FitrianitaAffiliation unknown1
Syahputra WibowoAffiliation unknown1
Bantari Wisynu Kusuma WardhaniAffiliation unknown1
Canggih Setya BudiAffiliation unknown1
Siahaan RafaelAffiliation unknown1
Waras NurcholisAffiliation unknown1
Eka Rahmat HidayatAffiliation unknown1
Yanuar PurwantoAffiliation unknown1

Affiliations come from OpenAlex; journal OAI-PMH metadata carries none. Authors without an OpenAlex ID are matched by name, which can merge or split people.

Metadata source: OAI-PMH (metadata jurnal) http://journal.ipb.ac.id/index.php/hayati/oai, first harvested 8 Nov 2026, last seen 8 Nov 2026.
Original metadata (oai_dc)
<oai_dc:dc xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/  http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
	<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>
</oai_dc:dc>