| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CALB |
| Uniprot No | P22676 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSSA EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M |
| 预测分子量 | 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CALB重组蛋白的3篇示例文献，涵盖表达优化、固定化应用及酶工程方向，结构参考实际研究主题：
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1. **文献名称**：High-level expression of Candida antarctica lipase B in Pichia pastoris through codon optimization and fermentation strategy
**作者**：Zhang Y. et al.
**摘要**：本研究通过密码子优化和调控启动子强度，在毕赤酵母中高效表达重组CALB。采用高密度发酵技术，酶活达到15.000 U/L，并验证了重组酶在酯合成中的催化效率，为工业化生产提供参考。
2. **文献名称**：Immobilization of recombinant CALB on functionalized silica nanoparticles for continuous biodiesel production
**作者**：Liu X. et al.
**摘要**：通过共价结合将重组CALB固定于氨基修饰的二氧化硅纳米颗粒，优化固定化条件后酶活性保留率达85%。在连续生物柴油生产中重复使用10次后仍保持70%活性，展现了良好的操作稳定性。
3. **文献名称**：Enhancing thermostability of Candida antarctica lipase B via computational design and directed evolution
**作者**：Wang T. et al.
**摘要**：结合分子动力学模拟与定向进化技术，对CALB进行突变改造。获得突变体Tm值提高8°C，在60°C下的半衰期延长3倍，显著提升了其在高温催化反应中的工业适用性。
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**备注**：上述文献为示例性内容，实际引用时建议通过学术数据库(如PubMed、Web of Science)检索真实发表的论文，并核对作者及摘要准确性。研究重点可围绕表达系统优化、固定化工艺、酶分子改造等方向展开。
**Background of CALB (Candida antarctica Lipase B) Recombinant Protein**
CALB, derived from the yeast *Candida antarctica*, is a highly versatile lipase widely utilized in biocatalysis. As a member of the α/β-hydrolase family, it features a conserved catalytic triad (Ser-His-Asp) embedded in a compact, thermostable structure. Unlike many lipases, CALB lacks a lid domain, granting it unique substrate accessibility and stability in diverse environments, including organic solvents and elevated temperatures (up to 60–70°C).
Recombinant CALB is produced via heterologous expression systems such as *E. coli*, *Pichia pastoris*, or filamentous fungi. These systems enable high-yield, cost-effective production while maintaining the enzyme’s catalytic efficiency and stereoselectivity. Its recombinant form is often engineered for enhanced properties, such as improved activity or tolerance to industrial conditions.
CALB’s broad substrate specificity and enantioselectivity make it invaluable in pharmaceuticals (e.g., synthesizing chiral intermediates), biofuels (transesterification for biodiesel), and fine chemicals (e.g., esters, amides). It is also employed in green chemistry for reducing waste and harsh reagents.
Advantages over chemical catalysts include mild reaction conditions, biodegradability, and reusability (via immobilization). Ongoing research focuses on protein engineering and immobilization techniques to expand its industrial applicability. CALB exemplifies the integration of enzymology and biotechnology to address sustainable manufacturing challenges.
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