Production of Angiotensin-I-Converting-Enzyme-Inhibitory Peptides in Fermented Milks (Lassi) Fermented by Lactobacillus acidophillus with Consideration of Incubation Period and Simmering Treatment

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• 作者：P. V. Padghan ; Bimlesh Mann ; Rajan Sharma…
• 关键词：Angiotensin converting enzyme (ACE) ; Lactic acid bacteria (LAB) ; Hippuryl ; l ; histidyl ; l ; leucine (HHL)
• 刊名：International Journal of Peptide Research and Therapeutics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：23
• 期：1
• 页码：69-79
• 全文大小：
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Biochemistry, general; Animal Anatomy / Morphology / Histology; Polymer Sciences; Pharmaceutical Sciences/Technology; Pharmacology/Toxicology; Molecular Medicine;
• 出版者：Springer Netherlands
• ISSN：1573-3904
• 卷排序：23

文摘

The lassi, fermented milks product containing angiotensin-I-converting-enzyme (ACE)-inhibitory peptides were produced by using selected Lactobacillus acidophilus NCDC-15 and the incubation period and simmering effect was also optimized for production of ACE-inhibitory peptides. The time–temperature combination for the heat treatment was optimized using RSM. The biological activity was measured in the supernatant of the fermented milk after centrifugation. The lowest IC₅₀ values for the inhibition of angiotensin-converting enzyme (ACE) was found 28.9 ± 0.95 μg protein/ml in the supernatant of milk fermented by L. acidophilus and heated at 78 °C for 10 h. The fractions which showed the highest ACE-inhibitory indexes were further purified by different techniques including solid phase extraction, RP-HPLC and FPLC and the related peptides were identified by LC–MS/MS using the Ultimate 3000 nano HPLC system (Dionex) coupled to a 4000 Q TRAP electro-spray ionization mass spectrometry. The high ACE-inhibitory activity containing fractions of the milk fermented by L. acidophilus contained the sequences of b-casein (b-CN) fragment. The fraction-III showed minimum IC₅₀ value i.e. 14.57 ± 0.72 μg/ml compared with fraction-I and fraction-II. Among these peptides 14 peptides have been identified from the fraction-I of the lassi prepared from L. acidophilus i.e. β-CN f47–56, β-CN f47–57, β-CN f199–209, β-CN f176–182, β-CN f176–183, β-CN f176–184, β-CN f1–7, β-CN f57–68, β-CN f166–175, β-CN f195–206, β-CN f195–207, β-CN f195–209, β-CN f94–106 and β-CN f169–176 showed partially or completely homology to that the milk protein bioactive peptides having ACE inhibitory. The two peptides KVLPVPQK (β-CN f169–176) and YQEPVLGPVRGPFPIIV (β-CN f193–209) have the same sequence as ACE inhibitory peptides (Maeno et al. in J Dairy Sci 79(8):1316–1321, 1996; Yamamoto et al. in J Dairy Sci 77:917–922, 1994b).