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Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production

Bulletin of Chemical Reaction Engineering & Catalysis · Vol. ume (2024) · hlm. 215–229

DOI
10.9767/bcrec.20130
ISSN
1978-2993
Terbit
2024-08-30
Penerbit
Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)
Bahasa
eng
Lisensi
creativecommons.org/licenses/by-sa/4.0

Abstrak

The low cost and excellent catalytic properties of lipase for industrial processes are highly desirable. A promising new approach involves the support modification of lipase and spacer arm, which enables the enhancement of lipase properties. This study investigates the immobilization of crude lipase from Mucor miehei onto a Polyurethane Foam (PUF) surface using various coating techniques. The PUF matrix was obtained through isocyanate and polyol reactions. Subsequently, the PUF was coated by adsorbing lipase and adding edible support material. The immobilized lipase was then utilized in the hydrolysis of coconut oil to produce fatty acids. Furthermore, the immobilized enzyme was employed in the esterification of fatty acids to produce bio-flavors. The results demonstrate that the attachment reaction using support material, namely lecithin, gelatin, MgCl2, and Polyethylene glycol 6000 (PEG), all of which are simple and edible, was able to enhance the stability and reusability of lipase. This immobilization technique increased triglyceride hydrolysis into FFA by 422%. The successful edible support modification of immobilized lipase from M. miehei on PUF, coupled with significantly enhanced enzyme stability and catalytic activity, offers a promising, environmentally friendly solution for diverse applications in the food industry. Copyright © 2024 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).

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  • Institut Teknologi Sepuluh Nopember
  • Universitas Jember
  • Politeknik Negeri Malang
  • University of Surabaya
  • Sriwijaya University
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Tampilkan sebagai tabel
Rekan penulisOrganisasiArtikel bersama
Nur FadhilahInstitut Teknologi Sepuluh Nopember10
Hanny F. SangianInstitut Teknologi Sepuluh Nopember6
Tantular NurtonoInstitut Teknologi Sepuluh Nopember6
Candra WijayaInstitut Teknologi Sepuluh Nopember4
Tri WidjajaInstitut Teknologi Sepuluh Nopember4
Lieke RiadiUniversity of Surabaya4
Siska Nuri FadilahSriwijaya University4
Bekti PalupiUniversitas Jember3
Meta Fitri RizkianaUniversitas Jember3
Ari Diana SusantiUniversitas Jember3
Setiyo GunawanInstitut Teknologi Sepuluh Nopember3
Silvya Yusnica AgnestyInstitut Teknologi Sepuluh Nopember2
Istiqomah RahmawatiUniversitas Jember2
Boy Arief FachriUniversitas Jember2
Felix Arie SetiawanUniversitas Jember2
Helda Wika AminiUniversitas Jember2
Atiqa RahmawatiUniversitas Jember2
Ditta Kharisma Yolanda PutriUniversitas Jember2
Urania Noor Lintang PertiwiInstitut Teknologi Sepuluh Nopember2
Tabina Raissa ApolInstitut Teknologi Sepuluh Nopember2
Ika Putri Nikmatur RohmahInstitut Teknologi Sepuluh Nopember2
Sukmawati RahmaAfiliasi tidak diketahui1
Junaidi KristianInstitut Teknologi Sepuluh Nopember1
Hellen Kartika DewiInstitut Teknologi Sepuluh Nopember1
Debra Arlin PuspasariInstitut Teknologi Sepuluh Nopember1
Niki EtrulyInstitut Teknologi Sepuluh Nopember1
Dyah SawitriInstitut Teknologi Sepuluh Nopember1
Ari AnggoroAfiliasi tidak diketahui1
Akbarningrum FatmawatiInstitut Teknologi Sepuluh Nopember1
Kamila Adila MuslimInstitut Teknologi Sepuluh Nopember1
Doty Dewi RisantiInstitut Teknologi Sepuluh Nopember1
Ruri Agung WahyuonoInstitut Teknologi Sepuluh Nopember1
Dendy SatrioInstitut Teknologi Sepuluh Nopember1

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Sumber metadata: OAI-PMH (metadata jurnal) https://journal.bcrec.id/index.php/bcrec/oai, pertama di-harvest 8 Nov 2026, terakhir terlihat 8 Nov 2026.
Metadata asli (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">Development of a Novel Support Modification for Efficient Lipase Immobilization: Preparation, Characterization, and Application for Bio-flavor Production</dc:title>
	<dc:creator>Moentamaria, Dwina</dc:creator>
	<dc:creator>Irfin, Zakijah</dc:creator>
	<dc:creator>Chumaidi, Achmad</dc:creator>
	<dc:creator>Widjaja, Arief</dc:creator>
	<dc:creator>Widjaja, Tri</dc:creator>
	<dc:creator>Muharja, Maktum</dc:creator>
	<dc:creator>Darmayanti, Rizki Fitria</dc:creator>
	<dc:subject xml:lang="en-US">Immobilization; Bioflavor; Mucor miehei lipase; Polyurethane foam; Support modification</dc:subject>
	<dc:description xml:lang="en-US">The low cost and excellent catalytic properties of lipase for industrial processes are highly desirable. A promising new approach involves the support modification of lipase and spacer arm, which enables the enhancement of lipase properties. This study investigates the immobilization of crude lipase from Mucor miehei onto a Polyurethane Foam (PUF) surface using various coating techniques. The PUF matrix was obtained through isocyanate and polyol reactions. Subsequently, the PUF was coated by adsorbing lipase and adding edible support material. The immobilized lipase was then utilized in the hydrolysis of coconut oil to produce fatty acids. Furthermore, the immobilized enzyme was employed in the esterification of fatty acids to produce bio-flavors. The results demonstrate that the attachment reaction using support material, namely lecithin, gelatin, MgCl2, and Polyethylene glycol 6000 (PEG), all of which are simple and edible, was able to enhance the stability and reusability of lipase. This immobilization technique increased triglyceride hydrolysis into FFA by 422%. The successful edible support modification of immobilized lipase from M. miehei on PUF, coupled with significantly enhanced enzyme stability and catalytic activity, offers a promising, environmentally friendly solution for diverse applications in the food industry. Copyright © 2024 by Authors, Published by BCREC Publishing Group. This is an open access article under the CC BY-SA License (https://creativecommons.org/licenses/by-sa/4.0).</dc:description>
	<dc:publisher xml:lang="en-US">Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)</dc:publisher>
	<dc:date>2024-08-30</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-US"></dc:type>
	<dc:format>application/pdf</dc:format>
	<dc:identifier>https://journal.bcrec.id/index.php/bcrec/article/view/20130</dc:identifier>
	<dc:identifier>10.9767/bcrec.20130</dc:identifier>
	<dc:source xml:lang="en-US">Bulletin of Chemical Reaction Engineering &amp; Catalysis; 2024: BCREC Volume 19 Issue 2 Year 2024 (August 2024); 215-229</dc:source>
	<dc:source>1978-2993</dc:source>
	<dc:language>eng</dc:language>
	<dc:relation>https://journal.bcrec.id/index.php/bcrec/article/view/20130/9698</dc:relation>
	<dc:relation>https://journal.bcrec.id/index.php/bcrec/article/downloadSuppFile/20130/5144</dc:relation>
	<dc:relation>https://journal.bcrec.id/index.php/bcrec/article/downloadSuppFile/20130/5145</dc:relation>
	<dc:rights xml:lang="en-US">Copyright (c) 2024 by Authors, Published by BCREC Publishing Group</dc:rights>
	<dc:rights xml:lang="en-US">https://creativecommons.org/licenses/by-sa/4.0</dc:rights>
</oai_dc:dc>