Efficient secretion of mussel adhesion proteins using a chaperone protein Spy as fusion tag in Bacillus subtilis
Efficient secretion of mussel adhesion proteins using a chaperone protein Spy as fusion tag in Bacillus subtilis
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DOI：
10.1002/biot.202200582
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发表时间：
2023-06
影响因子：
4.7
通讯作者：
Panpan Wu;Qing Tao;Yuxuan Liu;Caiting Zeng;Y. Li;Xin Yan
中科院分区：
文献类型：
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作者：
Panpan Wu;Qing Tao;Yuxuan Liu;Caiting Zeng;Y. Li;Xin Yan
贻贝足蛋白（Mfps）是一种特殊的蛋白质材料，具有很强的粘附能力。重组表达是大规模合成这些蛋白质的理想途径。然而，在异源宿主中尚未实现Mfps分泌表达到培养基中。
Mussel foot proteins (Mfps) are considered as remarkable materials due to their extraordinary adhesive capability. Recombinant expression is an ideal way to synthesis these proteins at large scale. However, secretory expression of Mfps into culture medium has not been achieved in a heterologous host.