| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | gox |
| Uniprot No | Q9UJM8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-370aa |
| 氨基酸序列 | MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMLPRLICINDYEQH AKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLST SVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSS IEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYL GNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAID PSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQ LDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVG RPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNP LAVSKI |
| 预测分子量 | 45 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. |
以下是关于GOX(葡萄糖氧化酶)重组蛋白的模拟参考文献示例，供参考：
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1. **《Enhanced production of recombinant glucose oxidase in Pichia pastoris》**
*Bankar, S.B., et al.*
摘要：研究比较了大肠杆菌、酿酒酵母和毕赤酵母表达系统对重组GOX产量的影响，发现毕赤酵母在优化培养基后产量提高3倍，并保持了高催化活性。
2. **《Immobilization of recombinant glucose oxidase for biosensor applications》**
*Liu, Y., et al.*
摘要：开发了一种基于纳米材料固定化重组GOX的方法，显著提高了生物传感器的稳定性和灵敏度，适用于血糖检测及工业过程监控。
3. **《Optimization of fermentation conditions for high-level expression of GOX in E. coli》**
*Zhang, Q., et al.*
摘要：通过响应面法优化大肠杆菌表达重组GOX的发酵条件，使酶活达到120 U/mg，为低成本规模化生产提供了方案。
4. **《Purification and characterization of recombinant glucose oxidase for electrochemical applications》**
*Raba, J., & Horozidian, S.*
摘要：报道了重组GOX的纯化工艺，并验证其在葡萄糖燃料电池中的高效电子传递能力，催化效率较天然酶提升40%。
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注：以上文献为示例性内容，实际引用时请核实真实文献信息及数据库来源(如PubMed、ScienceDirect等)。
**Background of Recombinant Glucose Oxidase (GOX)**
Glucose oxidase (GOX, EC 1.1.3.4) is an oxidoreductase enzyme naturally produced by fungi, such as *Aspergillus* and *Penicillium* species. It catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone while reducing molecular oxygen to hydrogen peroxide. This reaction has broad industrial relevance, driving interest in recombinant GOX production to meet high demand and ensure consistency.
Recombinant GOX is engineered via heterologous expression systems, typically using bacterial (e.g., *E. coli*), yeast (e.g., *Pichia pastoris*), or fungal hosts. These systems enable scalable production, improved enzyme purity, and customization of properties like thermostability or substrate specificity. For instance, codon optimization and promoter engineering enhance expression yields, while site-directed mutagenesis can tailor enzymatic activity for specific applications.
Structurally, GOX is a homodimeric glycoprotein with flavin adenine dinucleotide (FAD) as a prosthetic group. Its catalytic mechanism involves two steps: FAD-dependent glucose oxidation and reoxidation of FAD by oxygen. Recombinant versions often address limitations of native enzymes, such as glycosylation variability in fungal GOX, which can affect stability and activity.
Applications span biosensors (e.g., blood glucose monitoring), food preservation (oxygen removal and antimicrobial effects), and biotechnology (biofuel cells, diagnostic kits). In the food industry, recombinant GOX is preferred for its GRAS (Generally Recognized as Safe) status and efficiency in extending shelf life. Recent research focuses on immobilization techniques and fusion proteins to enhance reusability and functionality.
Overall, recombinant GOX exemplifies the synergy between enzymology and genetic engineering, offering sustainable solutions for healthcare, food technology, and industrial biocatalysis. Ongoing advancements in protein engineering and expression systems continue to expand its utility and efficiency.
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