Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal
An <i>Aspergillus niger</i> endo-1,4-β-mannanase, Man26A, was confirmed by FTIR and XRD to be immobilised on glutaraldehyde-activated chitosan nanoparticles via covalent bonding. The immobilisation (%) and activity yields (%) were 82.25% and 20.75%, respectively. The biochemical properti...
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| Format: | Article |
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MDPI AG
2022-11-01
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| Series: | Agronomy |
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| author | Amy S. Anderson Lithalethu Mkabayi Samkelo Malgas Naveen Kango Brett I. Pletschke |
| author_facet | Amy S. Anderson Lithalethu Mkabayi Samkelo Malgas Naveen Kango Brett I. Pletschke |
| author_sort | Amy S. Anderson |
| collection | DOAJ |
| description | An <i>Aspergillus niger</i> endo-1,4-β-mannanase, Man26A, was confirmed by FTIR and XRD to be immobilised on glutaraldehyde-activated chitosan nanoparticles via covalent bonding. The immobilisation (%) and activity yields (%) were 82.25% and 20.75%, respectively. The biochemical properties (pH, temperature optima, and stability) were then comparatively evaluated for both the free and immobilised Man26A. The optimal activity of Man26A shifted to a lower pH after immobilisation (pH 2.0–3.0, from pH 5 for the free enzyme), with the optimum temperature remaining unchanged (60 °C). The two enzymes exhibited identical thermal stability, maintaining 100% activity for the first 6 h at 55 °C. Substrate-specific kinetic analysis showed that the two enzymes had similar affinities towards locust bean gum (LBG) with varied <i>V<sub>max</sub></i> values. In contrast, they showed various affinities towards soybean meal (SBM) and similar <i>V<sub>max</sub></i> values. The immobilised enzyme was then employed in the enhancement of the functional feed/prebiotic properties of SBM from poultry feed, increasing mannooligosaccharides (MOS) quantities. The SBM main hydrolysis products were mannobiose (M2) and mannose (M1). The SBM-produced sugars could be utilised as a carbon source by probiotic bacteria; <i>Streptococcus thermophilus</i>, <i>Bacillus subtilis</i>, and <i>Lactobacillus bulgaricus</i>. The results indicate that the immobilised enzyme has the potential for use in the sustainable and cost-effective production of prebiotic MOS from agricultural biomass. |
| first_indexed | 2024-03-09T17:25:45Z |
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| language | English |
| last_indexed | 2024-03-09T17:25:45Z |
| publishDate | 2022-11-01 |
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| series | Agronomy |
| spelling | doaj.art-294fe5b13dd445b6a4c69fc6ada580f52023-11-24T12:44:36ZengMDPI AGAgronomy2073-43952022-11-011212299310.3390/agronomy12122993Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean MealAmy S. Anderson0Lithalethu Mkabayi1Samkelo Malgas2Naveen Kango3Brett I. Pletschke4Enzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Makhanda 6140, South AfricaEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Makhanda 6140, South AfricaDepartment of Biochemistry, Genetics and Microbiology, University of Pretoria, Hatfield 0028, South AfricaDepartment of Microbiology, Dr Harisingh Gour Vishwavidyalaya (A Central University), Sagar 470003, IndiaEnzyme Science Programme (ESP), Department of Biochemistry and Microbiology, Rhodes University, Makhanda 6140, South AfricaAn <i>Aspergillus niger</i> endo-1,4-β-mannanase, Man26A, was confirmed by FTIR and XRD to be immobilised on glutaraldehyde-activated chitosan nanoparticles via covalent bonding. The immobilisation (%) and activity yields (%) were 82.25% and 20.75%, respectively. The biochemical properties (pH, temperature optima, and stability) were then comparatively evaluated for both the free and immobilised Man26A. The optimal activity of Man26A shifted to a lower pH after immobilisation (pH 2.0–3.0, from pH 5 for the free enzyme), with the optimum temperature remaining unchanged (60 °C). The two enzymes exhibited identical thermal stability, maintaining 100% activity for the first 6 h at 55 °C. Substrate-specific kinetic analysis showed that the two enzymes had similar affinities towards locust bean gum (LBG) with varied <i>V<sub>max</sub></i> values. In contrast, they showed various affinities towards soybean meal (SBM) and similar <i>V<sub>max</sub></i> values. The immobilised enzyme was then employed in the enhancement of the functional feed/prebiotic properties of SBM from poultry feed, increasing mannooligosaccharides (MOS) quantities. The SBM main hydrolysis products were mannobiose (M2) and mannose (M1). The SBM-produced sugars could be utilised as a carbon source by probiotic bacteria; <i>Streptococcus thermophilus</i>, <i>Bacillus subtilis</i>, and <i>Lactobacillus bulgaricus</i>. The results indicate that the immobilised enzyme has the potential for use in the sustainable and cost-effective production of prebiotic MOS from agricultural biomass.https://www.mdpi.com/2073-4395/12/12/2993chitosanendo-1,4-β-mannanaseimmobilisationmannooligosaccharidesprebioticsoybean meal |
| spellingShingle | Amy S. Anderson Lithalethu Mkabayi Samkelo Malgas Naveen Kango Brett I. Pletschke Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal Agronomy chitosan endo-1,4-β-mannanase immobilisation mannooligosaccharides prebiotic soybean meal |
| title | Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal |
| title_full | Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal |
| title_fullStr | Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal |
| title_full_unstemmed | Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal |
| title_short | Covalent Immobilisation of an <i>Aspergillus niger</i> Derived Endo-1,4-β-Mannanase, Man26A, on Glutaraldehyde-Activated Chitosan Nanoparticles for the Effective Production of Prebiotic MOS from Soybean Meal |
| title_sort | covalent immobilisation of an i aspergillus niger i derived endo 1 4 β mannanase man26a on glutaraldehyde activated chitosan nanoparticles for the effective production of prebiotic mos from soybean meal |
| topic | chitosan endo-1,4-β-mannanase immobilisation mannooligosaccharides prebiotic soybean meal |
| url | https://www.mdpi.com/2073-4395/12/12/2993 |
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