Microorganisms
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2024
·Vol. 12
·期 7
·1381
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IF 4.1
Xuezhi Shao,Hongliang Fang,Tao Li,Liyan Yang,Dengfeng Yang,Lixia Pan
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of recalcitrant polysaccharides. There are limited reports on LPMOs capable of concurrently catalyzing the oxidative cleavage of both cellulose and chitin. In this study, we identified and cloned a novel LPMO from the newly isolated bacteriumChitinilyticum aquatileCSC-1, designated asCaLPMO10. When using 2, 6-dimethylphenol (2, 6-DMP) as the substrate,CaLPMO10 exhibited optimal activity at 50 °C and pH 8, demonstrating good temperature stability at 30 °C. Even after a 6 h incubation at pH 8 and 30 °C,CaLPMO10 retained approximately 83.03 ± 1.25% residual enzyme activity. Most metal ions were found to enhance the enzyme activity ofCaLPMO10, with ascorbic acid identified as the optimal reducing agent. Mass spectrometry analysis indicated thatCaLPMO10 displayed oxidative activity towards both chitin and cellulose, identifying it as a C1/C4-oxidized LPMO.CaLPMO10 shows promise as a key enzyme for the efficient utilization of biomass resources in future applications.
研究领域:
生物化学
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微生物学
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产品关联
DOI
PubMed
高影响因子
BIORESOURCE TECHNOLOGY
·
2022
·
IF 11.889
Fei Li,Yuxin Liu,Yang Liu,Yanjun Li,Hongbo Yu
Lytic polysaccharide monooxygenases could enhance the enzymatic conversion of recalcitrant polysaccharides by glycoside hydrolases. This study reports the expression and identification of a novel AA10 LPMO from Natrialbaceae archaeon , named Na LPMO10A, as a C1 oxidizer of chitin. The optimal temperature and pH for Na LPMO10A activity were 40 °C and 9.0, respectively, and Na LPMO10A exhibited high thermostability and pH stability under alkaline conditions. Na LPMO10A was also highly tolerant and stable when treated with high concentration of metal ions (1 M). Moreover, metal ions (Na + , K + , Ca 2+ and Mg 2+ ) significantly promoted Na LPMO10A activity and improved the saccharification efficiency of chitin by 22.6%, 45.9%, 36.7% and 53.9%, respectively, compared to commercial chitinase alone. Together, the findings of this study fill a gap in archaeal LPMO research, and for the first time demonstrate that archaeal Na LPMO10A could be a promising enzyme for improving saccharification under extreme condition, with potential applications in biorefineries.
研究领域:
生物化学
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酶工程
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微生物学
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产品关联
DOI
PubMed
高影响因子
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
·
2025
·
IF 8.5
Nan Zhang,Junaid Haider,Maxine Yew,Jianhua Yang,Leilei Zhu
Lytic polysaccharide monooxygenases (LPMOs) play a unique role in biomass saccharification as they catalyze oxidative cleavage of recalcitrant polysaccharides. Here, four new starch-active AA13 LPMOs were identified via phylogenetic analysis and functionally expressed in Pichia pastoris , followed by the investigation of oxidative activity towards different starch substrates. The four purified AA13 LPMOs were capable of oxidizing amylose, amylopectin and corn starch, generating soluble products. Among the four, Fv AA13, which exhibited the best oxidative activity, was further studied. Its yield of oxidized products was 1.9-fold, 1.4-fold, and 1.3-fold higher than the previously reported Nc AA13 when applied to starch substrates amylose, amylopectin, and corn starch, respectively. Furthermore, the oxidized product yield of Fv AA13 was enhanced by 2-fold when supplemented with 100 μM H 2 O 2 . Fv AA13 also enhanced the amylose degradation catalyzed by α-amylase and glucoamylase at 50 °C with an increment of the product by 1.4-fold and 1.9-fold, respectively. When combined with glucoamylase at a mass concentration ratio of 0.5:1 to 2:1, the reducing sugars released from the enzymatic degradation of amylopectin were improved by 4.5 to 9.7-fold compared to using glucoamylase alone. These findings underscored the substantial promoting effect of the supplementary Fv AA13 in amylolytic cocktails for starch saccharification.
研究领域:
生物化学
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酶学
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产品关联
DOI
PubMed
高影响因子
Biofuels Bioproducts & Biorefining-Biofpr
·
2023
·
IF 3.9
Yanping Xie,Xuekun Ma,Abdul Waheed,Muhammad Adnan,Ning Xie,Gang Liu
Cellobiose dehydrogenase (CDH) catalyzes the oxidation of cello-oligosaccharides and transfers electrons to oxygen or other electron receptors, such as lytic polysaccharide oxygenases (LPMOs). Cellobiose dehydrogenase has the potential to be used as an electron donor for LPMOs. Therefore, it is important to obtain CDHs under reaction conditions that are compatible with those of cellulases and LPMOs. Here, a CDH gene from Myceliophthora thermophila ( Mt CDH-A) was constitutively expressed in Trichoderma reesei , and its ability to donate electrons to the LPMO was validated. Mt CDH-A has an optimal pH of 6.0 and maintains relatively high activity over a wide pH range. The optimal temperature was 60°C, and it remained stable at 50°C for a long time. These enzymatic properties were compatible with the catalytic conditions of fungal LPMOs and cellulases. When Mt CDH-A was used as an electron donor, the synergistic effect of LPMO and cellulase improved the degradation efficiency of phosphoric acid-swollen cellulose by 141%. This work provides a novel insight into finding a stable electron donor for LPMOs and a new direction for finding more efficient thermostable CDHs in newly identified fungal species. © 2023 Society of Industrial Chemistry and John Wiley & Sons Ltd.
研究领域:
生物化学
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酶学
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微生物学
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DOI
高影响因子
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
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2021
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IF 5.279
Fei Li,Honglu Zhao,Ruijian Shao,Xiaoyu Zhang,Hongbo Yu
The Fenton reaction is considered to be of great significance in the initial attack of lignocellulose in wood-decaying fungi. Quinone redox cycling is the main way to induce the Fenton reaction in fungi. We show that lytic polysaccharide monooxygenases (LPMOs), through LPMO-catalyzed oxidation of hydroquinone, can efficiently cooperate with glucose dehydrogenase (GDH) to achieve quinone redox cycling. The LPMO/GDH system can enhance Fe3+-reducing activity, H2O2 production, and hydroxyl radical generation, resulting in a fueled Fenton reaction. The system-generated hydroxyl radicals exhibited a strong capacity to decolorize different synthetic dyes and degrade lignin. Our results reveal a potentially critical connection between LPMOs and the Fenton reaction, suggesting that LPMOs could be involved in xenobiotic compound and lignin degradation in fungi. This new role of LPMOs may be exploited for application in biorefineries.
研究领域:
微生物学
·
环境科学
·
生物化学
✓ 已验证
DOI
PubMed
高影响因子
危险品化学品经营许可证（带存储）