| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | melA |
| Uniprot No | O34645 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-432aa |
| 氨基酸序列 | MKKITFIGAGSTIFAKNVLGDCLLTEALNGFEFALYDIDPKRLQESQLMLENLRDRYNPSVAINSYDDRKLALQNAGYVINAIQVGGYKPSTVIDFEIPKRYGLRQTIADTVGIGGIFRSLRTIPVLFDIAKDMEEMCPDAWFLNYTNPMATLTGAMLRYTNIKTIGLCHSVQVCTKDLFKALGMEHDGIEERIAGINHMAWLLEVKKDGTDLYPEIKRRAKEKQKTKHHDMVRFELMDKFGYYVTESSEHNAEYHPYFIKRNYPELISELQIPLDEYPRRCVKQIENWEKMRDDIVNNKNLTHERSKEYGSRIIEAMETNEPFTFGGNVLNTGLITNLPSKAVVEVTCVADRKKITPCFAGELPEQLAALNRTNINTQLMTIEAAVTRKKEAVYQAAMLDPHTSAELSMKDIISMCDDLFAAHGDWLPEYK |
| 预测分子量 | 51.3 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. |
以下是关于melA重组蛋白的3篇文献示例(内容基于学术文献常见主题虚构，供参考)：
1. **文献名称**：*Heterologous expression and characterization of α-galactosidase melA from Bacillus subtilis in E. coli*
**作者**：Li, X., Zhang, Y., Wang, H.
**摘要**：该研究在大肠杆菌中成功表达了来自枯草芽孢杆菌的melA基因编码的α-半乳糖苷酶，优化了诱导条件(如IPTG浓度和温度)，并证明重组酶在60℃和pH 6.0时活性最高，可高效降解豆科植物中的棉子糖类抗营养因子。
2. **文献名称**：*Enhanced thermostability of recombinant melA α-galactosidase through site-directed mutagenesis for industrial applications*
**作者**：Chen, J., Liu, R., Park, S.
**摘要**：通过理性设计对melA酶进行定点突变(如Tyr-120→Phe)，提高了其热稳定性(70℃下半衰期延长3倍)，并验证了突变体在饲料添加剂中降解大豆寡糖的应用潜力。
3. **文献名称**：*High-level production of recombinant melA in Pichia pastoris and its application in raffinose hydrolysis*
**作者**：Guo, L., Wang, T., Fernández-Lucas, J.
**摘要**：利用毕赤酵母系统高效表达melA蛋白，通过发酵优化使酶产量达到120 U/mL，并证明该重组酶在甜菜糖蜜加工中可有效水解棉子糖，提高蔗糖产率。
(注：以上文献为模拟示例，实际引用需检索PubMed、Web of Science或Google Scholar等平台，以真实发表论文为准。)
MelA recombinant protein is derived from the melA gene, which encodes α-galactosidase, an enzyme that catalyzes the hydrolysis of α-1.6-linked galactose residues in oligosaccharides such as raffinose and stachyose. This enzyme is of significant interest due to its role in breaking down indigestible carbohydrates, particularly in legume-based foods and animal feed, where these oligosaccharides contribute to flatulence and reduced nutrient absorption. Originally identified in microorganisms, including lactic acid bacteria and *Bacillus* species, the melA gene has been heterologously expressed in recombinant systems like *E. coli* or yeast to enable scalable production of the enzyme for industrial applications.
The development of recombinant MelA leverages genetic engineering to enhance enzyme yield, stability, and activity under specific conditions. In the food industry, it is used to process legumes (e.g., soy products) to reduce anti-nutritional factors, improving digestibility. In animal feed, MelA supplementation boosts feed efficiency by degrading complex sugars. Biotechnological applications include the synthesis of functional oligosaccharides and glycoconjugates. Medically, α-galactosidase has therapeutic potential for Fabry disease, a genetic disorder caused by deficiencies in endogenous α-galactosidase activity.
Recent research focuses on optimizing MelA through protein engineering, such as improving thermostability for high-temperature processing or tailoring substrate specificity. Structural studies using X-ray crystallography and computational modeling have provided insights into its catalytic mechanism, guiding rational design. Additionally, microbial fermentation systems for MelA production are being refined to meet industrial demands for cost-effective, sustainable enzyme production. These advancements position recombinant MelA as a versatile tool in biotechnology, agriculture, and medicine, addressing challenges in nutrition, health, and industrial processes.
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