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Thermophilic Xylanase Production Rom Isolates of Macula’ Hot Springs Bacteria Using Corn Cobs Waste Media

Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta) · Vol. ume No. 2 (2019) · pp. 25–41

DOI
10.70561/ica.v10i2.6652
ISSN
2655-6049, 2085-014X
Published
2019-05-30
Publisher
Hasanuddin University
Language
en

Abstract

Xylanases is an extracellular enzyme that has prospects as enzymes that hydrolyze hemicellulose (xylan). In this study, carried out isolatied of bacteria from the hot springs Makula', Tana Toraja and determine the optimum conditions in producing the xylanase enzyme. The steps being taken are the rejuvenation of bacteria, the manufacture medium inoculum and the production medium, the measurement OD (Optical Density) measurements of protein and testing activities xylanase. The results obtained showed that the production time for B. stearothermophilus SL3A is in the 48 hours with a value of 0.1237 activity mU/mL and B. stearothermophilus SL3S at the 60 hours with a value of 0.1593 activity mU/mL. B. stearothermophilus SL3A have a protein content of 9.828 mg/mL and for B. stearothermophilus SL3S have a protein content of 10.07 mg/mL. Characteristics bacterial xylanase from B. stearothermophilus SL3A and B. stearothermophilus SL3S work optimally at pH 7 a temperature of 45 ºC. Crude extract of the isolated xylanase enzyme can hydrolyze substrate is xylan corn cobs. The addition of metal CaCl2, MgCl2, CaCl2 can increase the activities of the enzyme xylanase and CoCl2 decreases the activities of enzymes that are inhibitors.

Keywords

Collaboration network of the authors

40 authors · 99 co-authorship links · showing the 40 most connected

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  • Universitas Muhammadiyah Buton
  • Affiliation unknown
  • Different organisations
  • Same organisation
  • Affiliation unknown
  • Thicker line = more joint articles · bigger circle = more articles
Show as table
Co-authorOrganisationJoint articles
Ahyar AhmadAffiliation unknown6
Abdur Rahman ArifAffiliation unknown4
Sartika DanialAffiliation unknown4
Muhammad ZakirAffiliation unknown3
Muawanah MuawanahAffiliation unknown2
Ischaidar IschaidarAffiliation unknown2
Hanapi UsmanAffiliation unknown2
Leliani LelianiAffiliation unknown2
Leliani RamliAffiliation unknown2
ABDUL KARIMAffiliation unknown2
Alfian Nasir MaidinAffiliation unknown2
Rugaiyah A ArfahAffiliation unknown1
St Fauziah St FauziahAffiliation unknown1
Prastawa BudiAffiliation unknown1
Indah RayaAffiliation unknown1
Erna MayasariAffiliation unknown1
Nursiah La NafieAffiliation unknown1
Sabaniah Indjar GamaAffiliation unknown1
Paulina TabaAffiliation unknown1
Fatahu FatahuAffiliation unknown1
Sarwina HafidAffiliation unknown1
Firdaus FirdausAffiliation unknown1
Nunuk Hariani SoekamtoAffiliation unknown1
Selfi WullurAffiliation unknown1
Rauf PatongAffiliation unknown1
Muhammad Noor DjalaluddinAffiliation unknown1
Pirman APAffiliation unknown1
Adriani AdrianiAffiliation unknown1
Emmi AstutiAffiliation unknown1
Sulfiani SulfianiAffiliation unknown1
Nursyamsi NursyamsiAffiliation unknown1
Fitriani BUniversitas Muhammadiyah Buton1
Nur AsmiAffiliation unknown1
Harningsih KarimAffiliation unknown1
Ali MuhakimAffiliation unknown1
Siti KhairunnurAffiliation unknown1
Nur HaedarAffiliation 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) https://journal.unhas.ac.id/index.php/ica/oai, first harvested 5 Nov 2026, last seen 5 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">Thermophilic Xylanase Production Rom Isolates of Macula’ Hot Springs Bacteria Using Corn Cobs Waste Media</dc:title>
	<dc:creator xml:lang="en">Denta Putri, Lupita</dc:creator>
	<dc:creator xml:lang="en">Natsir, Hasnah</dc:creator>
	<dc:creator xml:lang="en">Dali, Seniwati</dc:creator>
	<dc:subject xml:lang="en">Bacillus stearothermophilus</dc:subject>
	<dc:subject xml:lang="en">xylan</dc:subject>
	<dc:subject xml:lang="en">xylanases</dc:subject>
	<dc:description xml:lang="en">Xylanases is an extracellular enzyme that has prospects as enzymes that hydrolyze hemicellulose (xylan). In this study, carried out isolatied of bacteria from the hot springs Makula', Tana Toraja and determine the optimum conditions in producing the xylanase enzyme. The steps being taken are the rejuvenation of bacteria, the manufacture medium inoculum and the production medium, the measurement OD (Optical Density) measurements of protein and testing activities xylanase. The results obtained showed that the production time for B. stearothermophilus SL3A is in the 48 hours with a value of 0.1237 activity mU/mL and B. stearothermophilus SL3S at the 60 hours with a value of 0.1593 activity mU/mL. B. stearothermophilus SL3A have a protein content of 9.828 mg/mL and for B. stearothermophilus SL3S have a protein content of 10.07 mg/mL. Characteristics bacterial xylanase from B. stearothermophilus SL3A and B. stearothermophilus SL3S work optimally at pH 7 a temperature of 45 ºC. Crude extract of the isolated xylanase enzyme can hydrolyze substrate is xylan corn cobs. The addition of metal CaCl2, MgCl2, CaCl2 can increase the activities of the enzyme xylanase and CoCl2 decreases the activities of enzymes that are inhibitors. </dc:description>
	<dc:publisher xml:lang="en">Hasanuddin University</dc:publisher>
	<dc:date>2019-05-30</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>https://journal.unhas.ac.id/index.php/ica/article/view/6652</dc:identifier>
	<dc:identifier>10.70561/ica.v10i2.6652</dc:identifier>
	<dc:source xml:lang="en">Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta); Volume 10, No.2: December 2017; 25-41</dc:source>
	<dc:source>2655-6049</dc:source>
	<dc:source>2085-014X</dc:source>
	<dc:language>en</dc:language>
	<dc:relation>https://journal.unhas.ac.id/index.php/ica/article/view/6652/3625</dc:relation>
	<dc:rights xml:lang="en">Copyright (c) 2017 Jurnal Akta Kimia Indonesia (Indonesia Chimica Acta)</dc:rights>
</oai_dc:dc>