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Enzyme Secretion
EditEnzyme secretion designates the directed translocation of an enzyme from its cytoplasmic site of synthesis across the cell envelope into the extracellular environment or, in eukaryotic cells, into the lumen of the secretory pathway. The defining molecular requirement is an N-terminal signal peptide that routes the polypeptide to the Sec translocon or an alternative export machinery, where translocation occurs and the signal peptide is subsequently removed by signal peptidase [1][2]. In biotechnology, the term encompasses native export of hydrolytic enzymes by microbial production hosts and engineered secretion of homologous or heterologous enzymes into the culture medium [3][4]. Essential components include the target enzyme, a compatible signal sequence, the membrane-embedded translocation apparatus, and accessory chaperones and processing proteases that maintain secretion competence [2][5]. Secretion efficiency is governed by compatibility among the signal peptide, the mature enzyme sequence, and host quality-control checkpoints along the export route [1][3].
References
- Roland Freudl; Signal Peptides for Recombinant Protein Secretion in Bacterial Expression Systems. Microb. Cell Fact. 2018, 17, 1-10. [CrossRef]
- Alexandra Tsirigotaki; Jozefien De Geyter; Nikolina Šoštaric´; Anastassios Economou; Spyridoula Karamanou; Protein Export through the Bacterial Sec Pathway. Nat. Rev. Microbiol. 2016, 15, 21-36. [CrossRef]
- Ken-Ichi Yoshida; Jan Maarten van Dijl; Engineering Bacillus subtilis Cells as Factories: Enzyme Secretion and Value-added Chemical Production. Biotechnol. Bioprocess Eng. 2020, 25, 872-885. [CrossRef]
- Mette Lübeck; Peter Stephensen Lübeck; Fungal Cell Factories for Efficient and Sustainable Production of Proteins and Peptides. Microorganisms 2022, 10, 753. [CrossRef]
- Sonia Gullón; Rafael P. Mellado; The Cellular Mechanisms that Ensure an Efficient Secretion in Streptomyces. Antibiotics 2018, 7, 33. [CrossRef]
