Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents
Dump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also ex...
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MDPI AG
2025-04-01
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| Series: | Fermentation |
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| author | Mfezeko Noxhaka Nonso E. Nnolim Lindelwa Mpaka Uchechukwu U. Nwodo |
| author_facet | Mfezeko Noxhaka Nonso E. Nnolim Lindelwa Mpaka Uchechukwu U. Nwodo |
| author_sort | Mfezeko Noxhaka |
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| description | Dump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also examined the crude lipase’s ability to remove stains from cotton fabric. Among twelve bacteria isolated, five demonstrated notable halo zones on tributyrin agar plates. The diameters (mm) were MN38 (11 ± 1.4), MN1310 (8.5 ± 0.7), MN28 (6.5 ± 0.71), MN18 (7.0 ± 1.4), and MN310 (8.15 ± 0.21). Quantitative analysis revealed that MN38 exhibited the highest lipase activity (14.76 ± 0.27 U/mL), while MN1310 showed the lowest (6.40 ± 0.85 U/mL). Nucleotide sequence analysis identified the isolates as <i>Raoultella terrigena</i> veli18 (MN38), <i>Stenotrophomonas maltophilia</i> veli96 (MN1310), <i>Viridibacillus</i> sp. veli10 (MN28), <i>Stenotrophomonas</i> sp. veli19 (MN18), and <i>Klebsiella</i> sp. veli70 (MN310). The crude lipase from <i>R. terrigena</i> veli18 maintained 73.33%, 52.67%, 55.0%, and 54.0% of its original activity after 60 min of exposure to Sunlight, Surf, Maq, and Omo, respectively. Adding crude lipase to enzyme-free laundry detergents significantly enhanced their cleaning efficacy, completely removing oil stains from cotton fabric. This performance of <i>R. terrigena</i> veli18 crude lipase highlights its potential as an effective detergent bio-additive. |
| format | Article |
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| institution | OA Journals |
| issn | 2311-5637 |
| language | English |
| publishDate | 2025-04-01 |
| publisher | MDPI AG |
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| series | Fermentation |
| spelling | doaj-art-2464b6f9abe4492f91aed5cdf0be8aad2025-08-20T02:17:20ZengMDPI AGFermentation2311-56372025-04-0111422510.3390/fermentation11040225Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance DetergentsMfezeko Noxhaka0Nonso E. Nnolim1Lindelwa Mpaka2Uchechukwu U. Nwodo3Patho-Biocatalysis Group (PBG), Department of Biotechnology and Biological Sciences, University of Fort Hare, Private Bag X1314, Alice 5700, Eastern Cape, South AfricaPatho-Biocatalysis Group (PBG), Department of Biotechnology and Biological Sciences, University of Fort Hare, Private Bag X1314, Alice 5700, Eastern Cape, South AfricaPatho-Biocatalysis Group (PBG), Department of Biotechnology and Biological Sciences, University of Fort Hare, Private Bag X1314, Alice 5700, Eastern Cape, South AfricaPatho-Biocatalysis Group (PBG), Department of Biotechnology and Biological Sciences, University of Fort Hare, Private Bag X1314, Alice 5700, Eastern Cape, South AfricaDump sites harbour microorganisms with potential for environmentally friendly industrial applications. This study assessed the lipolytic activity of municipal dumpsite-associated bacteria and evaluated the stability of the most potent isolate’s lipolytic enzyme against laundry detergents. It also examined the crude lipase’s ability to remove stains from cotton fabric. Among twelve bacteria isolated, five demonstrated notable halo zones on tributyrin agar plates. The diameters (mm) were MN38 (11 ± 1.4), MN1310 (8.5 ± 0.7), MN28 (6.5 ± 0.71), MN18 (7.0 ± 1.4), and MN310 (8.15 ± 0.21). Quantitative analysis revealed that MN38 exhibited the highest lipase activity (14.76 ± 0.27 U/mL), while MN1310 showed the lowest (6.40 ± 0.85 U/mL). Nucleotide sequence analysis identified the isolates as <i>Raoultella terrigena</i> veli18 (MN38), <i>Stenotrophomonas maltophilia</i> veli96 (MN1310), <i>Viridibacillus</i> sp. veli10 (MN28), <i>Stenotrophomonas</i> sp. veli19 (MN18), and <i>Klebsiella</i> sp. veli70 (MN310). The crude lipase from <i>R. terrigena</i> veli18 maintained 73.33%, 52.67%, 55.0%, and 54.0% of its original activity after 60 min of exposure to Sunlight, Surf, Maq, and Omo, respectively. Adding crude lipase to enzyme-free laundry detergents significantly enhanced their cleaning efficacy, completely removing oil stains from cotton fabric. This performance of <i>R. terrigena</i> veli18 crude lipase highlights its potential as an effective detergent bio-additive.https://www.mdpi.com/2311-5637/11/4/225detergent formulationenvironmental sustainabilitygreen chemistrylipolytic enzyme<i>Raoultella terrigena</i> |
| spellingShingle | Mfezeko Noxhaka Nonso E. Nnolim Lindelwa Mpaka Uchechukwu U. Nwodo Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents Fermentation detergent formulation environmental sustainability green chemistry lipolytic enzyme <i>Raoultella terrigena</i> |
| title | Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents |
| title_full | Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents |
| title_fullStr | Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents |
| title_full_unstemmed | Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents |
| title_short | Biocatalytic Potential of a <i>Raoultella terrigena</i>-Derived Lipolytic Enzyme for High-Performance Detergents |
| title_sort | biocatalytic potential of a i raoultella terrigena i derived lipolytic enzyme for high performance detergents |
| topic | detergent formulation environmental sustainability green chemistry lipolytic enzyme <i>Raoultella terrigena</i> |
| url | https://www.mdpi.com/2311-5637/11/4/225 |
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