Browse > Article

Angiotensin Ⅰ Converting Enzyme(ACE) Inhibitory Activities of Laver(Porphyra tenera) Protein Hydrolysates  

Kim Young-Myoung (Korea Food Research Institute)
Do Jeong-Ryong (Korea Food Research Institute)
In Jae-Pyung (Korea Food Research Institute)
Park Jong-Hyuk (Korea Food Research Institute)
Publication Information
The Korean Journal of Food And Nutrition / v.18, no.1, 2005 , pp. 11-18 More about this Journal
Abstract
Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.
Keywords
Laver(Porphyra tenera) hydrolysate; ACE inhibitory activity; protease; molecular fraction; drying method;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Lee, HO. Separation and purification of angiotensin I converting enzyme inhibitory peptide from algae hydrolysate., Dept. Food Nutr. Graduate School. Hanyang univesity. 1999
2 Jung, KJ, Jung, BM and Kim, SB. Effect of porphyran Isolated from laver, Porphyra yezoensis, on lipid metabolism in hyperlipidemic and hypercholesterolemic rats. Korean J. Food Sci. Technol. 33:633-640. 2001
3 Kim, SJ, Moon, JS, Kang, SG and Jung, ST. Exraction of porphyran from decolored laver. Korean J. Food Sci. Technol. 35:1017-1021. 2003
4 Kang, DG, Lee, YS, Kim, HJ, Lee, YM and Lee, HS. Angiotension converting enzyme inhibitory phenylpropanoid glycosides from Clerodendron trichotomum. J. Ethnopharma. 89: 151-154. 2003   DOI   ScienceOn
5 Hwang, JH. Angiotensin- I converting enzyme inhibitory effect of Doenjang fermented by B. subtillis SCB-3 isolated from Meju, Korean traditional food. J. Kor. Soc. Food Sci. Nutr. 26:775-783. 1997
6 Park, DC, Park, JH, Gu, YS, Han, JH, Byun, DS, Kim, EM, Kim, YM and Kim, SB. Efeects of salted fermented fish products and their alternatives on anigiotensin converting enzyme inhibitory activity of Kimchi during fermentation. Korean J. Food Sci. Technol. 32:920-927. 2000
7 Moon, SH, Ha, SC, Lee, DS, Kim, JG and Hong, SD. Identification and culture condition of an actinomycetes strain producing an angiotensin converting enzyme inhibitor. Kor. J. Appl. Micriobiol. Biotechnol. 23:439-445. 1995
8 A.O.A.C. Official Methods of Analysis, 16th ed., Chapter 11. pp. 1-31. The Association of Official Analytical Chemists, Washington, DC. 1998
9 Maruyama, S, Nakagomi, K, Tomizuka, N and Suzuki, H. Angiotensin converting enzyme inhibitor derived from an enzymatic hydrolysate of casein. Agric. Biol. Chem. 49: 1405-1410. 1985   DOI
10 Kunio, S. Purification and identification of angiotensin I -converting enzyme inhibitors from the red alga Porphyra yezoensis. J. Mar. Biotechnol. 6: 163-167. 1998
11 Furneaux, RH, Miller, IJ, and Stevenson, TT. Agaroids from New Zealand members of the Gracilariaceae( Gracilariales, Rhodophyta )-a novel dimethylated agar. Hydrobiologia.204:645-650. 1990   DOI
12 Cheung, HS and Chshman, DW. Spectrometric assay and proterties of angiotensin coverting enzyme of rabbit lung. Biochem. Phamacol. 20:1637-1647. 1971   DOI   ScienceOn
13 Kinoshita, E, Yamakoshi, J and Kikuchi, M. Purification and identification of an angiotensin- I converting enzyme inhibitor from soy sauce. Bio. Biotech. Biochem. 57: 1107-1110. 1993   DOI   ScienceOn
14 Dodgson, KS and Price, RG. A note on the determination of the esther sulphate content of sulphated polysaccharides. J. Biochem. 84:106-107. 1962   DOI
15 Cushman, DW and Ondetti, MA. In progress in Medicinal Chemistry. pp.41. Elsevier, North Holland, Amsterdam. 1979
16 Hong, SP, Kim, MH and Oh, SW. ACE inhibitory and antihypertensive effect of chitos oligosaccaharide in SHR. Korean J. Food Sci. Technol. 30:1476-1479. 1998
17 Lee, KH, Song, SH and Jeong, IH. Quality changes of dried lavers during processing and storage. Bull. Korean Fish. Soc. 20:408-418. 1987
18 Park, JH, Koo, JG, Do, JR, Yang, CB and Woo, SK. Effect of extraction temperature and pH on the chemical properties of crude porpyran extracted from Porphyra yezoensis. J. Korean Fish. Soc. 31: 127131. 1998
19 Kim, TJ, Yoon, HD, Lee, DS, Jang, YS, Sub, SB and Yeum, DM. Angiotensin I converting enzyme inhigitory activity of hot-water extract and enzymatic hydrolysate of freash water fish. J. Korean Soc. Food Sci. Nutr. 25:871-877. 1996
20 Koo, JG and Park, JH. Chemical and gelling properties of alkali-modified porphyran. J. Korean Fish. Soc. 32:271-275. 1999
21 Ryu, IW and Shin, YS. Inhibition effect of ACE (angiotensin coverting enzyme) and kinetics of aloe acethylmannan. Korean J. Food Sci. Technol. 29: 1269-1274. 1997
22 Engel, SL, Schaeffer, TR, Gold, BI and Rubin, B. Inhibition of pressure effects of agiotensin I and augmentation of depressor effects of bradykinin by synthetic peptides. Proc. Soc. Exp. Biol. Med. 140: 240-245. 1972
23 Maruyama, S, Mitachi, H, Tankata, H, Tomizuka, N, and Suzuki, H. Studies on the active site and antihypertensive activity of angiotensin I converting enzyme inhibitors derived from casein. Agic. Biol. Chem. 51:1581-1586. 1987   DOI
24 Dubois, M, Gills, KA, Hamilton, JK, Rebers, PA, and Smith, F. Colorimetric method for the determination of sugars and related substances. Anal. Chem. 28:350-352. 1956   DOI
25 Jo, KS, Do, JR and Koo, JG. Pretreatment condition of Porphyra yezoensis, Undaria pinnatifida and Laminaria religiosa for functional alage-tea. J. Korean Soc. Food Sci. Nutr. 27:275-280. 1998