| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | AAO |
| Uniprot No | P24792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-579aa |
| 氨基酸序列 | SQIRHYKWEVEYMFWAPDCNENIVMGINGQFPGPTIRANAGDTVVVELINKLHTEGVVIHWHGILQRGTPWADGTASISQCAINPGETFFYNFTVDNPGTFFYHGHLGMQRSAGLYGSLIVDPPQGKKEPFHYDGEINLLLSDWWHQSIHKQEVGLSSKPIRWIGEPQTILLNGRGQFDCSIAAKYDSNLEPCKLKGSEPCAPYIFHVMPKKTYRIRIASTTALAALNFAIGNHPLLVVEADGNYVQPFYTSDIDIYSGESYSVLITTDQNPSENYWVSVGTRGRHPNTPPGLTLLNYLPNSVSKLPTSPPPETPAWDDFDRSKNFTYRITAAMGSPKPPVKSNRRIFLLNTQNVINGYVKWAINDVSLALPPTPYLGAMKFNLLHAFDQNPPPEVFPEDYDIDTPPTNEKTKIGNGVYQFKIGEIVDVILQNANMMKENLSEIHPWHLHGHDFWVLGYGDGKFTAEEESSLNLKNPPLRNTVVIFPYGWTAIRFVADNPGVWAFHCHIEPHLHMGMGVVFAEGVEKVGRIPTKALACGGTAKSLINNP |
| 预测分子量 | 74.3 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于AAO(Aryl-alcohol oxidase，芳基醇氧化酶)重组蛋白的参考文献及其摘要概括：
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1. **标题**：*"Heterologous expression of aryl-alcohol oxidase from *Pleurotus eryngii* in *Escherichia coli*: purification and characterization"*
**作者**：Guillén F, et al.
**摘要**：研究报道了通过大肠杆菌异源表达来自*Pleurotus eryngii*真菌的AAO，并优化纯化步骤获得高活性重组酶，分析了其催化特性及在木质素降解中的作用。
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2. **标题**：*"Engineering a thermostable aryl-alcohol oxidase for enhanced oxidative biocatalysis"*
**作者**：Ferreira P, et al.
**摘要**：通过定点突变技术改造AAO的热稳定性，获得耐受高温的重组酶，验证其在工业催化中(如生物燃料生产)的应用潜力。
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3. **标题**：*"Functional expression of a fungal aryl-alcohol oxidase in *Pichia pastoris* and its use in enzymatic synthesis of chiral compounds"*
**作者**：Ruiz-Dueñas FJ, et al.
**摘要**：利用毕赤酵母系统高效表达重组AAO，证明其催化芳基醇转化为醛类的能力，并用于手性化合物的绿色合成。
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(注：若需扩展，可补充其他相关研究，如AAO在生物传感器或环境污染物降解中的应用文献。)
**Background of AAO Recombinant Protein**
Aryl alcohol oxidase (AAO), a flavin-dependent enzyme, plays a critical role in the oxidative degradation of lignin and aromatic compounds, primarily in ligninolytic fungi such as *Pleurotus* species. It catalyzes the oxidation of aromatic alcohols to corresponding aldehydes while reducing molecular oxygen to hydrogen peroxide (H₂O₂), which supports lignin breakdown by peroxidases. This enzymatic activity positions AAO as a key player in natural carbon cycling and industrial bioprocesses, particularly in biofuel production, bioremediation, and pulp biobleaching.
Traditional extraction of AAO from native fungal sources faces challenges, including low yield, time-consuming cultivation, and contamination risks. Recombinant protein technology offers a solution by enabling the heterologous expression of AAO in controlled microbial systems (e.g., *E. coli*, yeast, or filamentous fungi). Through genetic engineering, the AAO gene is cloned into expression vectors, optimized for codon usage, and expressed in high-density fermentation setups. This approach enhances protein yield, purity, and scalability while reducing production costs.
Recombinant AAO retains catalytic efficiency and substrate specificity, with potential improvements in stability or activity through protein engineering. Its applications extend to biosensors, organic synthesis, and enzyme cocktails for lignocellulosic biomass conversion. However, challenges remain, such as achieving proper folding of the multi-domain structure and balancing redox cofactor requirements in heterologous hosts. Ongoing research focuses on optimizing expression systems, fusion tags, and fermentation conditions to unlock AAO’s full industrial potential in sustainable biotechnology.
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