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

Process Biochem.. 2011-11;  46(11):2205-2209
A Gildberg, JA Arnesen, BS Sæther, J Rauø, Even Stenberg. Nofima Marin, Norwegian Institute of Food, Fisheries and Aquaculture Research, P.O. Box 6122, NO-9291 Tromsø, Norway.
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摘要

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, IC50 = 0.075 and 0.035 mg/ml, respectively, than earlier reported in comparable hydrolysates. Two novel ACE inhibitory tri-peptides, Phe-Thr-Tyr (IC50 = 275 and 59 μM) and Phe-Ser-Tyr (IC50 = 7.7 and 2.2 μM), 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, th... More

关键词

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