Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1
Relatively little is known about enzymes with broad substrate spectra, leading to limited applications and progress. Herein, we elucidate Aly16-1 of <i>Streptomyces</i> sp. strain CB16 as a novel multifunctional member of the eighth polysaccharide lyase (PL8) family, although it shared f...
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2024-11-01
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| author | Lianghuan Zeng Junge Li Jingyan Gu Wei Hu Wenjun Han Yuezhong Li |
| author_facet | Lianghuan Zeng Junge Li Jingyan Gu Wei Hu Wenjun Han Yuezhong Li |
| author_sort | Lianghuan Zeng |
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| description | Relatively little is known about enzymes with broad substrate spectra, leading to limited applications and progress. Herein, we elucidate Aly16-1 of <i>Streptomyces</i> sp. strain CB16 as a novel multifunctional member of the eighth polysaccharide lyase (PL8) family, although it shared few sequence identities with the characterized enzymes. The recombinant enzyme rAly16-1 showed lyase activities against several acidic polysaccharides, including many glycosaminoglycan types, xanthan, and alginate. It was mannuronate (M)-preferred, endolytic, and optimal at 50 °C and pH 6.0. The smallest substrate was an ∆M-terminal (∆: unsaturated monosaccharide) trisaccharide, and the minimal product was ∆. In the final alginate digestions by rAly16-1, the fractions larger than disaccharides were ∆G-terminal (G: guluronate), while the disaccharides were mainly ∆M, showing an oligosaccharide-yielding property under the succession law. However, when degrading various oligosaccharides, rAly16-1 continued producing ∆M from the non-reducing end even when the substrates increased their sizes, quite different from the elucidated alginate lyases with variable alginate-degrading modes. Thus, co-determined by its M-preference, Aly16-1 is novel for its ∆M-yielding property in oligosaccharide preparations. Additionally, rAly16-1 can be applied in sequencing unsaturated trisaccharides, whether ∆M- or ∆G-terminal. This study provides novel insights into the characteristics and applications of a multifunctional enzyme within the PL8 family for resource explorations. |
| format | Article |
| id | doaj-art-9c72d8adddc64ea697b79ddec59ce126 |
| institution | OA Journals |
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| language | English |
| publishDate | 2024-11-01 |
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| series | Microorganisms |
| spelling | doaj-art-9c72d8adddc64ea697b79ddec59ce1262025-08-20T02:04:59ZengMDPI AGMicroorganisms2076-26072024-11-011211237410.3390/microorganisms12112374Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1Lianghuan Zeng0Junge Li1Jingyan Gu2Wei Hu3Wenjun Han4Yuezhong Li5National Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaUnited Post Graduate Education Base of Shandong University and Jinan Enlighten Biotechnology Co., Ltd., Jinan 250101, ChinaNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaNational Glycoengineering Research Center, Shandong Key Laboratory of Carbohydrate Chemistry and Glycobiology, NMPA Key Laboratory for Quality Research and Evaluation of Carbohydrate-Based Medicine, State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, ChinaRelatively little is known about enzymes with broad substrate spectra, leading to limited applications and progress. Herein, we elucidate Aly16-1 of <i>Streptomyces</i> sp. strain CB16 as a novel multifunctional member of the eighth polysaccharide lyase (PL8) family, although it shared few sequence identities with the characterized enzymes. The recombinant enzyme rAly16-1 showed lyase activities against several acidic polysaccharides, including many glycosaminoglycan types, xanthan, and alginate. It was mannuronate (M)-preferred, endolytic, and optimal at 50 °C and pH 6.0. The smallest substrate was an ∆M-terminal (∆: unsaturated monosaccharide) trisaccharide, and the minimal product was ∆. In the final alginate digestions by rAly16-1, the fractions larger than disaccharides were ∆G-terminal (G: guluronate), while the disaccharides were mainly ∆M, showing an oligosaccharide-yielding property under the succession law. However, when degrading various oligosaccharides, rAly16-1 continued producing ∆M from the non-reducing end even when the substrates increased their sizes, quite different from the elucidated alginate lyases with variable alginate-degrading modes. Thus, co-determined by its M-preference, Aly16-1 is novel for its ∆M-yielding property in oligosaccharide preparations. Additionally, rAly16-1 can be applied in sequencing unsaturated trisaccharides, whether ∆M- or ∆G-terminal. This study provides novel insights into the characteristics and applications of a multifunctional enzyme within the PL8 family for resource explorations.https://www.mdpi.com/2076-2607/12/11/2374alginatedegradation patternglycosaminoglycanmultifunctionaloligosaccharide preparationpolysaccharide lyase family |
| spellingShingle | Lianghuan Zeng Junge Li Jingyan Gu Wei Hu Wenjun Han Yuezhong Li Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 Microorganisms alginate degradation pattern glycosaminoglycan multifunctional oligosaccharide preparation polysaccharide lyase family |
| title | Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 |
| title_full | Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 |
| title_fullStr | Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 |
| title_full_unstemmed | Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 |
| title_short | Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1 |
| title_sort | alginate degrading modes oligosaccharide yielding properties and potential applications of a novel bacterial multifunctional enzyme aly16 1 |
| topic | alginate degradation pattern glycosaminoglycan multifunctional oligosaccharide preparation polysaccharide lyase family |
| url | https://www.mdpi.com/2076-2607/12/11/2374 |
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