Angiotensin I-converting enzyme inhibitory activity in a hydrolysate of proteins from Northern shrimp (Pandalus borealis) and identification of two novel inhibitory tri-peptides

作者：Gildberg A**jorn^*; Arnesen Jan Arne; Saether Bjorn Steinar; Rauo Jaran; Stenberg Even

来源：Process Biochemistry, 2011, 46(11): 2205-2209.

DOI：10.1016/j.procbio.2011.08.003

• Shrimp protein hydrolysate
• Pandalus borealis
• ACE inhibitory activity
• Nutraceutical

The ACE inhibitory activity of a desalted protein hydrolysate from Northern shrimp (Pandalus borealis) was studied. Measurements by two independent methods both revealed higher in vitro ACE inhibitory activity, IC(50) = 0.075 and 0.035 mg/ml, respectively, than earlier reported in comparable hydrolysates. Two novel ACE inhibitory tri-peptides, Phe-Thr-Tyr (IC(50) = 275 and 59 mu M) and Phe-Ser-Tyr (IC(50) = 7.7 and 2.2 mu M), were detected in the hydrolysate. An introductory feeding trial with spontaneously hypertensive rats indicated positive in vivo results when the rats were given 60 mg hydrolysate/kg body weight per day. Although further in vivo studies are necessary to verify the antihypertensive potential, the very high in vitro ACE inhibitory activity reveals that the shrimp protein hydrolysate is a promising candidate for nutraceutical application.

• 出版日期2011-11