Optimization of catalytic properties of Mucor racemosus lipase through immobilization in a biocompatible alginate gelatin hydrogel matrix for free fatty acid production: a sustainable robust biocatalyst for ultrasound-assisted olive oil hydrolysis
Abstract Immobilization is a key technology that improves the operational stability of enzymes. In this study, alginate-gelatin (Alg-Gel) hydrogel matrix was synthesized and used as immobilization support for Mucor racemosus lipase (Lip). Enzyme catalyzed ultrasound-assisted hydrolysis of olive oil was also investigated. Alg-Gel matrix exhibited high entrapment efficiency (94.5%) with a degradation rate of 42% after 30 days. The hydrolysis of olive oil using Alg-Gel-Lip increased significantly (P < 0.05) as compared to free Lip. Optimum pH and temperature were determined as pH 5.0 and 40 °C, respectively. The Vmax values for free and immobilized Lip were determined to be 5.5 mM and 5.8 mM oleic acid/min/ml, respectively, and the Km values were 2.2 and 2.58 mM/ml respectively. Thermal stability was highly improved for Alg-Gel-Lip ($ t_{1/2} $ 650 min and Ed 87.96 kJ/mol) over free Lip ($ t_{1/2} $ 150 min and Ed 23.36 kJ/mol). The enzymatic activity of Alg-Gel-Lip was preserved at 96% after four consecutive cycles and 90% of the initial activity after storage for 60 days at 4 °C. Alg-Gel-Lip catalyzed olive oil hydrolysis using ultrasound showed a significant (P < 0.05) increase in hydrolysis rate compared to free Lip (from 0.0 to 58.2%, within the first 2 h). In contrast to traditional methodology, using ultrasonic improved temperature-dependent enzymatic catalyzed reactions and delivered greater reaction yields. Results suggest that Alg-Gel-Lip biocatalyst has great industrial application potential, particularly for free fatty acid production. In addition, the combined use of enzyme and ultrasound has the potential of eco-friendly technology..
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2022 |
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Erschienen: |
2022 |
Enthalten in: |
Zur Gesamtaufnahme - volume:12 |
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Enthalten in: |
3 Biotech - 12(2022), 11 vom: 19. Sept. |
Sprache: |
Englisch |
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Beteiligte Personen: |
Abdel-Mageed, Heidi Mohamed [VerfasserIn] |
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Links: |
Volltext [kostenfrei] |
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Themen: |
Alginate gelatin hydrogel |
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Anmerkungen: |
© The Author(s) 2022 |
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doi: |
10.1007/s13205-022-03319-8 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
SPR048147028 |
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520 | |a Abstract Immobilization is a key technology that improves the operational stability of enzymes. In this study, alginate-gelatin (Alg-Gel) hydrogel matrix was synthesized and used as immobilization support for Mucor racemosus lipase (Lip). Enzyme catalyzed ultrasound-assisted hydrolysis of olive oil was also investigated. Alg-Gel matrix exhibited high entrapment efficiency (94.5%) with a degradation rate of 42% after 30 days. The hydrolysis of olive oil using Alg-Gel-Lip increased significantly (P < 0.05) as compared to free Lip. Optimum pH and temperature were determined as pH 5.0 and 40 °C, respectively. The Vmax values for free and immobilized Lip were determined to be 5.5 mM and 5.8 mM oleic acid/min/ml, respectively, and the Km values were 2.2 and 2.58 mM/ml respectively. Thermal stability was highly improved for Alg-Gel-Lip ($ t_{1/2} $ 650 min and Ed 87.96 kJ/mol) over free Lip ($ t_{1/2} $ 150 min and Ed 23.36 kJ/mol). The enzymatic activity of Alg-Gel-Lip was preserved at 96% after four consecutive cycles and 90% of the initial activity after storage for 60 days at 4 °C. Alg-Gel-Lip catalyzed olive oil hydrolysis using ultrasound showed a significant (P < 0.05) increase in hydrolysis rate compared to free Lip (from 0.0 to 58.2%, within the first 2 h). In contrast to traditional methodology, using ultrasonic improved temperature-dependent enzymatic catalyzed reactions and delivered greater reaction yields. Results suggest that Alg-Gel-Lip biocatalyst has great industrial application potential, particularly for free fatty acid production. In addition, the combined use of enzyme and ultrasound has the potential of eco-friendly technology. | ||
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700 | 1 | |a Gohary, Nesrine Abdelrehim E. L. |0 (orcid)0000-0001-6909-164X |4 aut | |
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