Melola Discovery

← Melola Discovery

Journal SINTA 1

Optimization and Characterization of Urease Immobilization from Red Lentil Seeds (Lens culinaris) Using Chitosan

Molekul: Jurnal Ilmiah Kimia · Vol. 20 No. 2 (2025) · pp. 268–278

DOI
10.20884/1.jm.2025.20.2.13134
ISSN
2503-0310, 1907-9761
Published
2025-07-24
Publisher
Universitas Jenderal Soedirman
Language
eng

Abstract

ABSTRACT. Urease is an enzyme that plays a vital role in catalyzing the hydrolysis of urea into ammonia (NH3) and carbon dioxide (CO2). This study focuses on the isolation of urease from red lentil seeds, followed by its immobilization. The objective of this research is to optimize and characterize urease that has been immobilized using chitosan and activated with glutaraldehyde. Red lentil seeds were processed with a mortar and pestle at low temperatures (4 °C) to obtain a crude enzyme extract, which was then concentrated using 50% acetone (P50) prior to immobilization. The optimization process for P50 urease immobilization involved assessing various factors, including chitosan concentration, glutaraldehyde concentration, temperature, and the immersion duration in glutaraldehyde. The findings revealed that the optimal conditions for immobilizing P50 urease were achieved at a chitosan concentration of 0.75%, with a 2% glutaraldehyde soak at 25 °C for 2 hours, resulting in an enzyme activity of 7.042 U/g. The immobilized P50 urease demonstrated the ability to be reused up to 7 times while maintaining 51% of its initial activity. Scanning Electron Microscopy (SEM) analysis indicated morphological changes in the beads after the addition of glutaraldehyde and the enzyme, shifting from a rounded to an irregular shape. Additionally, Fourier Transform Infrared Spectroscopy (FTIR) analysis identified C-N and C=N peaks, confirming the successful incorporation of glutaraldehyde. Keywords: immobilization, red lentil seeds, glutaraldehyde, chitosan, urease

Collaboration network of the authors

40 authors · 140 co-authorship links · 57 across different organisations · showing the 40 most connected

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

  • Jenderal Soedirman University
  • National Research and Innovation Agency
  • Islamic University of Riau
  • IPB University
  • Padjadjaran University
  • Universitas Islam Negeri Ar-Raniry
  • Sumatera Institute of Technology
  • Other organisations
  • Affiliation unknown
  • Different organisations
  • Same organisation
  • Affiliation unknown
  • Thicker line = more joint articles · bigger circle = more articles
Show as table
Co-authorOrganisationJoint articles
Mardiyah KurniasihJenderal Soedirman University4
Aprilia Nafi NurainiJenderal Soedirman University4
Uyi SulaemanJenderal Soedirman University3
Aris HaryadiJenderal Soedirman University2
Anung RiapanitraJenderal Soedirman University2
Istinganatun KhoeriyahAffiliation unknown2
Elinur ElinurIslamic University of Riau1
Hamdi AgustinIslamic University of Riau1
KUSWANDI KUSWANDIAffiliation unknown1
I Made ArtikaIPB University1
AHMAD ENDANG ZAINAL HASANIPB University1
Bejo HaryantoJenderal Soedirman University1
Nur FitriantoNational Research and Innovation Agency1
Salfa Athallah Agtari NabillahNational Research and Innovation Agency1
Roidah Cahya WatiJenderal Soedirman University1
Siti NurmilahPadjadjaran University1
Andri FrediansyahNational Research and Innovation Agency1
A. ArifinHasanuddin University1
Jamrud AminuddinJenderal Soedirman University1
Nurhayati NurhayatiUniversitas Islam Negeri Ar-Raniry1
Agustina WidiyaniSumatera Institute of Technology1
Mukhtar EffendiJenderal Soedirman University1
Abdullah Nur AzizJenderal Soedirman University1
Pakhrur RaziUniversitas Negeri Padang1
Wihantoro WihantoroJenderal Soedirman University1
Farzand AbdullatifJenderal Soedirman University1
Sunardi SunardiJenderal Soedirman University1
Yohannes SardjonoNational Nuclear Energy Agency of Indonesia1
Yaser KasesazNuclear Science and Technology Research Institute1
Ratna Stia DewiJenderal Soedirman University1
Kasandra BudiarniNational Research and Innovation Agency1
Dadan HermawanJenderal Soedirman University1

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://jos.unsoed.ac.id/index.php/jm/oai, first harvested 9 Nov 2026, last seen 9 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-US"> Optimization and Characterization of Urease Immobilization from Red Lentil Seeds (Lens culinaris) Using Chitosan</dc:title>
	<dc:creator>zusfahair, zusfahair</dc:creator>
	<dc:creator>Ningsih, Dian Riana</dc:creator>
	<dc:creator>Bilalodin, Bilalodin</dc:creator>
	<dc:creator>Fatoni, Amin</dc:creator>
	<dc:creator>Luthfia, Adilla</dc:creator>
	<dc:creator>Purwati, Purwati</dc:creator>
	<dc:creator>Muslihah, Niken Istikhari</dc:creator>
	<dc:creator>Apriliadina, Inessa Putri</dc:creator>
	<dc:description xml:lang="en-US">ABSTRACT. Urease is an enzyme that plays a vital role in catalyzing the hydrolysis of urea into ammonia (NH3) and carbon dioxide (CO2). This study focuses on the isolation of urease from red lentil seeds, followed by its immobilization. The objective of this research is to optimize and characterize urease that has been immobilized using chitosan and activated with glutaraldehyde. Red lentil seeds were processed with a mortar and pestle at low temperatures (4 °C) to obtain a crude enzyme extract, which was then concentrated using 50% acetone (P50) prior to immobilization. The optimization process for P50 urease immobilization involved assessing various factors, including chitosan concentration, glutaraldehyde concentration, temperature, and the immersion duration in glutaraldehyde. The findings revealed that the optimal conditions for immobilizing P50 urease were achieved at a chitosan concentration of 0.75%, with a 2% glutaraldehyde soak at 25 °C for 2 hours, resulting in an enzyme activity of 7.042 U/g. The immobilized P50 urease demonstrated the ability to be reused up to 7 times while maintaining 51% of its initial activity. Scanning Electron Microscopy (SEM) analysis indicated morphological changes in the beads after the addition of glutaraldehyde and the enzyme, shifting from a rounded to an irregular shape. Additionally, Fourier Transform Infrared Spectroscopy (FTIR) analysis identified C-N and C=N peaks, confirming the successful incorporation of glutaraldehyde.
&amp;nbsp;
Keywords: immobilization, red lentil seeds, glutaraldehyde, chitosan, urease</dc:description>
	<dc:publisher xml:lang="en-US">Universitas Jenderal Soedirman</dc:publisher>
	<dc:date>2025-07-24</dc:date>
	<dc:type>info:eu-repo/semantics/article</dc:type>
	<dc:type>info:eu-repo/semantics/publishedVersion</dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://jos.unsoed.ac.id/index.php/jm/article/view/13134</dc:identifier>
	<dc:identifier>10.20884/1.jm.2025.20.2.13134</dc:identifier>
	<dc:source xml:lang="en-US">Molekul; Vol 20 No 2 (2025); 268-278</dc:source>
	<dc:source>2503-0310</dc:source>
	<dc:source>1907-9761</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://jos.unsoed.ac.id/index.php/jm/article/view/13134/7159</dc:relation>
</oai_dc:dc>