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Production of novel angiotensin I-converting enzyme inhibitory peptides by fermentation of marine shrimp Acetes chinensis with Lactobacillus fermentum SM 605

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Abstract

Acetes chinensis is an underutilized shrimp species thriving in Bo Hai Gulf of China. Its hydrolysate digested with protease SM98011 has been previously shown to have high angiotensin I-converting enzyme (ACE) inhibitory activity (He et al., J Pept Sci 12:726–733, 2006). In this article, A. chinensis were fermented by Lactobacillus fermentum SM 605 and the fermented sauce presented high ACE inhibitory activity. The minimum IC50 value (3.37 ± 0.04 mg/mL) was achieved by response surface methodology with optimized process parameters such as fermentation time of 24.19 h, incubation temperature at 38.10°C, and pH 6.12. Three ACE inhibitory peptides are purified by ultrafiltration, gel filtration, and reverse-phase high performance liquid chromatography. Identified by mass spectrometry, their amino acid sequences are Asp-Pro, Gly-Thr-Gly, and Ser-Thr, with IC50 values of 2.15 ± 0.02, 5.54 ± 0.09, and 4.03 ± 0.10 μM, respectively. Also, they are all novel ACE inhibitory peptides. Compared with protease digestion, fermentation is a simpler and cheaper method to produce ACE inhibitory peptides from shrimp A. chinensis.

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Acknowledgment

This work was supported by grants from the National High Technology Research and Development Program of China (Nos. 2001AA625040 and 2003AA625040).

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Correspondence to Yu-Zhong Zhang.

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Wang, Y., He, H., Chen, X. et al. Production of novel angiotensin I-converting enzyme inhibitory peptides by fermentation of marine shrimp Acetes chinensis with Lactobacillus fermentum SM 605. Appl Microbiol Biotechnol 79, 785–791 (2008). https://doi.org/10.1007/s00253-008-1489-z

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Keywords

  • Angiotensin I-converting enzyme (ACE)
  • ACE inhibitory peptides
  • Antihypertensive
  • Acetes chinensis
  • Lactobacillus fermentum
  • Fermentation