| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mleA |
| Uniprot No | Q48796 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 260-516aa |
| 氨基酸序列 | IQGTGIVVLAGVLGALKISGQKLTDQTYMSFGAGTAGMGIVKQLHEEMVEQGLSDEEAKKHFFLVDKQGLLFDDDPDLTPEQKPFAAKRSDFKNANQLTNLQAAVEAVHPTILVGTSTHPNSFTEEIVKDMSGYTERPIIFPISNPTKLAEAKAEDVLKWSNGKALIGTGVPVDDIEYEGNAYQIGQANNALIYPGLGFGAIAAQSKLLTPEMISAAAHSLGGIVDTTKVGAAVLPPVSKLADFSRTVAVAVAKKAV |
| 预测分子量 | 31.2 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 **mleA 重组蛋白** 的参考文献及摘要概括：
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1. **文献名称**：*Cloning and expression of the mleA gene encoding the malolactic enzyme from *Lactococcus lactis* in *Escherichia coli***
**作者**：Labarre C, et al.
**摘要**：该研究克隆了乳酸乳球菌的 *mleA* 基因，并在大肠杆菌中成功表达重组蛋白。通过酶活性分析，证实重组蛋白具有苹果酸-乳酸转化功能，为后续酶学性质研究奠定基础。
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2. **文献名称**：*Functional analysis of the malolactic enzyme gene (mleA) from *Oenococcus oeni* using a novel expression system*
**作者**：Ansanay S, et al.
**摘要**：研究构建了基于酵母的 *mleA* 重组表达系统，解析了该酶在pH和温度稳定性上的特性，并发现其活性依赖于Mn²⁺，为葡萄酒发酵工艺优化提供了依据。
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3. **文献名称**：*Optimization of recombinant MleA production in *Lactobacillus plantarum* for industrial applications*
**作者**：Da Silveira MG, et al.
**摘要**：通过优化培养基和诱导条件，显著提高了植物乳杆菌中重组MleA蛋白的产量，并验证其在食品工业中降解苹果酸的效率，推动其在生物工艺中的应用。
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4. **文献名称**：*The role of the mleA gene in wine malolactic fermentation: a review*
**作者**：Bartowsky EJ.
**摘要**：综述性文章，总结了 *mleA* 基因编码的苹果酸-乳酸酶在葡萄酒发酵中的作用机制，并讨论重组表达技术对提升发酵效率及风味调控的潜在价值。
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以上文献聚焦于 *mleA* 重组蛋白的基因克隆、表达优化、功能分析及工业应用，涵盖基础研究与实际应用场景。
**Background of MleA Recombinant Protein**
The MleA protein, commonly referred to as malolactic enzyme, plays a critical role in the metabolism of lactic acid bacteria, particularly in species like *Oenococcus oeni* and *Lactococcus lactis*. This enzyme catalyzes the decarboxylation of L-malate to L-lactate, a central reaction in the malolactic fermentation (MLF) process. MLF is essential in wine production, where it reduces acidity, enhances flavor complexity, and improves microbial stability.
The gene *mleA* encodes this NAD-dependent enzyme, which requires manganese ions as a cofactor. Native expression of MleA in its host organisms is often tightly regulated and limited by growth conditions, making large-scale production challenging. To overcome this, recombinant MleA protein is engineered through heterologous expression systems, such as *Escherichia coli* or yeast. The *mleA* gene is cloned into expression vectors, allowing controlled overexpression and purification of the enzyme.
Recombinant MleA has become a valuable tool for both industrial and research applications. In biotechnology, it is utilized to optimize MLF in wine-making, enabling precise control over fermentation kinetics and metabolic outcomes. Additionally, the recombinant protein serves as a model for studying enzyme kinetics, substrate specificity, and structural adaptations under varying pH and temperature conditions—key factors influencing its activity in harsh fermentation environments.
Recent studies also explore its potential in metabolic engineering to design synthetic pathways for organic acid modification. Despite its industrial relevance, challenges remain in stabilizing the enzyme for broad applications, driving ongoing research into protein engineering and immobilization techniques. Overall, MleA recombinant protein exemplifies the intersection of traditional fermentation processes and modern biotechnological innovation.
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