Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability
Chitin is the second most prevalent polysaccharide found in nature, following cellulose. Amino-oligosaccharides, the byproducts of chitin degradation, exhibit favorable biological properties and potential for various uses. Chitinases play a crucial function in the breakdown of chitin, and their exce...
Saved in:
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2024-09-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/29/18/4302 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850260129842200576 |
|---|---|
| author | Mati Ullah Yutong Xia Dalal Sulaiman Alshaya Jianda Han Kotb A. Attia Tawaf Ali Shah Huayou Chen |
| author_facet | Mati Ullah Yutong Xia Dalal Sulaiman Alshaya Jianda Han Kotb A. Attia Tawaf Ali Shah Huayou Chen |
| author_sort | Mati Ullah |
| collection | DOAJ |
| description | Chitin is the second most prevalent polysaccharide found in nature, following cellulose. Amino-oligosaccharides, the byproducts of chitin degradation, exhibit favorable biological properties and potential for various uses. Chitinases play a crucial function in the breakdown of chitin, and their exceptionally effective production has garnered significant interest. Here, in this study, the exochitinase PbChiA, obtained from <i>Paenibacillus barengoltzii</i>, was recombinantly produced and immobilized using the CotG surface protein of <i>Bacillus subtilis</i> WB800N. The resulting strain <i>Bacillus subtilis</i> WB800N pHS-CotG-Chi exhibited exceptional heat stability and efficacy across various pH levels. The chitinolytic activity of the enzyme, which had been isolated and immobilized on the spore surface, was measured to be approximately 16.06 U/mL. Including Ni<sup>2+</sup>, Zn<sup>+2</sup>, and K<sup>+</sup>, and EDTA at various concentration levels in the reaction system, has significantly enhanced the activity of the immobilized enzyme. The immobilized exochitinase demonstrated a notable rate of recycling, as the recombinant spores sustained a relative enzyme activity of more than 70% after three cycles and 62.7% after four cycles. These findings established a basis for additional investigation into the role and practical use of the immobilized bacterial exochitinase in industry. |
| format | Article |
| id | doaj-art-af16fe9aca1442f1b7dacba5f3f84b07 |
| institution | OA Journals |
| issn | 1420-3049 |
| language | English |
| publishDate | 2024-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj-art-af16fe9aca1442f1b7dacba5f3f84b072025-08-20T01:55:42ZengMDPI AGMolecules1420-30492024-09-012918430210.3390/molecules29184302Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and RecyclabilityMati Ullah0Yutong Xia1Dalal Sulaiman Alshaya2Jianda Han3Kotb A. Attia4Tawaf Ali Shah5Huayou Chen6School of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaSchool of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaDepartment of Biology, College of Science, Princess Nourah bint Abdulrahman University, P.O. Box 84428, Riyadh 11671, Saudi ArabiaSchool of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaCenter of Excellence in Biotechnology Research, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi ArabiaCollege of Agriculture Engineering and Food Science, Shandong University of Technology, Zibo 255000, ChinaSchool of Life Sciences, Jiangsu University, Zhenjiang 212013, ChinaChitin is the second most prevalent polysaccharide found in nature, following cellulose. Amino-oligosaccharides, the byproducts of chitin degradation, exhibit favorable biological properties and potential for various uses. Chitinases play a crucial function in the breakdown of chitin, and their exceptionally effective production has garnered significant interest. Here, in this study, the exochitinase PbChiA, obtained from <i>Paenibacillus barengoltzii</i>, was recombinantly produced and immobilized using the CotG surface protein of <i>Bacillus subtilis</i> WB800N. The resulting strain <i>Bacillus subtilis</i> WB800N pHS-CotG-Chi exhibited exceptional heat stability and efficacy across various pH levels. The chitinolytic activity of the enzyme, which had been isolated and immobilized on the spore surface, was measured to be approximately 16.06 U/mL. Including Ni<sup>2+</sup>, Zn<sup>+2</sup>, and K<sup>+</sup>, and EDTA at various concentration levels in the reaction system, has significantly enhanced the activity of the immobilized enzyme. The immobilized exochitinase demonstrated a notable rate of recycling, as the recombinant spores sustained a relative enzyme activity of more than 70% after three cycles and 62.7% after four cycles. These findings established a basis for additional investigation into the role and practical use of the immobilized bacterial exochitinase in industry.https://www.mdpi.com/1420-3049/29/18/4302bacterial exochitinase<i>Bacillus substilis</i> WB800Nspore surface display |
| spellingShingle | Mati Ullah Yutong Xia Dalal Sulaiman Alshaya Jianda Han Kotb A. Attia Tawaf Ali Shah Huayou Chen Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability Molecules bacterial exochitinase <i>Bacillus substilis</i> WB800N spore surface display |
| title | Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability |
| title_full | Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability |
| title_fullStr | Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability |
| title_full_unstemmed | Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability |
| title_short | Display of Bacterial Exochitanase on <i>Bacillus subtilis</i> Spores Improved Enzyme Stability and Recyclability |
| title_sort | display of bacterial exochitanase on i bacillus subtilis i spores improved enzyme stability and recyclability |
| topic | bacterial exochitinase <i>Bacillus substilis</i> WB800N spore surface display |
| url | https://www.mdpi.com/1420-3049/29/18/4302 |
| work_keys_str_mv | AT matiullah displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT yutongxia displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT dalalsulaimanalshaya displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT jiandahan displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT kotbaattia displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT tawafalishah displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability AT huayouchen displayofbacterialexochitanaseonibacillussubtilisisporesimprovedenzymestabilityandrecyclability |