Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-convert...
Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.
Seven brown algal species (Ecklonia cava, Ishige okamurae, Sargassum fulvellum, Sargassum horneri, Sargassum coreanum, Sargassum thunbergii and Scytosiphon lomentaria) were hydrolyzed using five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and screened for angiotensin 1-converting enzyme (ACE) inhibitory activities. Most algal species examined showed good ACE inhibitory activities after the enzymatic hydrolysis. However, E. cava was the most potent ACE inhibitor of the seven species. Flavourzyme digest of E. cava exhibited an $IC_{50}$ of around $0.3\;{\mu}g/mL$ for ACE; captopril has an $IC_{50}$ of $\~0.05\;{\mu}g/mL$. The Flavourzyme digest was separated to three fractions by an ultrafiltration membrane (5, 10, 30 kDa MWCO) system according to the molecular weights. The active components were mainly concentrated in >30 kD fraction which are composed of the highest protein content $(27\%)$ and phenolic content (261 mg/100 mL) compared to the other two smaller molecular weight fractions. Therefore, the active compounds appear to be relatively high molecular weight complex molecules associated with protein (glycoprotein) and polyphenols. Therefore, E. cave is a potential source of antihypertensive compound.
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가설 설정
2) Values are mean±SD of two determinations and the sample concentration is 1 mg/mL.
제안 방법
ACE inhibitory activity was assayed by the method of Cushman and Chung (21) with slight modifications. HHL was dissolved in 100 mM sodium borate buffer, pH 8.
Since ail algal water extracts contained ACE inhibitory compounds, those samples were then subjected to enzymatic hydrolysis using five proteases (Protamex, Koji- zyme, Neutrase, Flavourzyme and Alcalase). After enzymatic hydrolysis of those algal species, they were then again evaluated for ACE inhibitory assay (Table 2). Most algal species in this study showed superior potential ACE inhibition after enzymatic hydrolysis.
Enzymatic hydrolysates are therefore specific and tailor- made for each application (25). Consistent with those previous observations, this study also obtained different activities after enzymatic hydrolyses. This fact may be due to different physiochemical conditions of the reaction mixture.
cava. In order to characterize the molecular weight of the active fraction, the Flavour- zyme digest of E. cava was passed through ultrafiltration membranes (5, 10 and 30 kD) and relevant molecular weight cut-off fractions were separated and evaluated for ACE inliibition. The molecular weight of the hydrolysate is one of the most important factors in producing protein hydrolysates with the desired functional properties to use as functional materials (27).
In this study, seven brown algal species (E. cava, I. okamurae, S. julvellum, S. horneri, S. coreanum, S. thunbergii and S. lomentaria) were hydrolyzed using five commercially available proteases: Protamex, Kojizyme, Neu- trase, Flavourzyme and Alcalase, and their hydrolysates were screened to evaluate their antihypertensive activities.
cava exhibited relatively higher ACE active compounds. Therefore, dose-dependent activity of protein hydrolysates from E. cava was evaluated in order to examine the exact lC5o value of each sample, and the IC50 values of the extracts were compared with that of captopril.
대상 데이터
In this study, water extracts of seven brown algal species were screened for their potential ACE inhibitory activities. ACE inhibitory activities of water extracts from seven brown al응al species (E.
이론/모형
The amount of crude protein was determined by the Lowry method, absorbance at 540 nm using brovine serum albumin as the calibration standard (20).
성능/효과
As has been mentioned in previous experiments, Fla- vourzyme has been used to prepare hydrolysates from com 이니tein (27) and ACE inhibitory active fractions have been obtained followed by ultrafiltration membranes. The results of that study indicated that separation of hydrolysates based on molecular weight distinctly enhanced the ACE inhibitory activity. Also, there are reports of the presence of high molecular weight protein (22~24 kD) called “oligomers” with potential ACE inhibitory activity.
This fact may be due to different physiochemical conditions of the reaction mixture. When we evaluate all results of this study, it is clear that all enzymatic extracts of E. cava exhibited relatively higher ACE active compounds. Therefore, dose-dependent activity of protein hydrolysates from E.
후속연구
cava might form some type of complex associated with proteins or glycoproteins and have ACE inhibitory activity. Therefore, further experiments are needed to evaluate the exact bioactive compound.
cava was weaker than captopril, further purification may improve its activity, even as a crude extract it has a great potential in ACE inhibition. Therefore, separation of pure active compounds from the Flavorzyme hydrolysate of E. cava is required for further studies.
참고문헌 (32)
Kohama Y, Oka H, Kayamori Y, Tsujikawa K, Mimura T, Nagase Y, Satake M. 1991. Potent synthetic analogues of angiotensin-converting enzyme inhibitor derived from tuna muscle. Agric Biol Chem 55: 2169-2170
Suetsuna K. 1992. Study on the inhibitory activities against angiotensin I-converting enzyme of the peptides derived from sardine muscle. PhD Dissertation. Tokoku University, Miyagi, Sendai, Japan. p 1-92
Isono Y. 1996. Peptide inhibitors for angiotensin I-converting enzyme from Masai fermented milk. Food Sci Technol Int 2: 213-216
Kato H, Suzuki T. 1971. Bradykinin-potentiating peptides from the venom of Agkistrodon halys blomhoffii: Isolation of five bradykinin potentiators Band C. Biochem 10: 972-980
Sawayama T, Itokawa A, Shimada K, Doi Y, Kimura K, Nishimura H. 1990. Synthesis of 1-[(s)-3-acetylthio-2-methylpropanoyl]-L-propyl-L-phenylalanine (Alacepril) and one of its active metabolites, the desacetyl derivative (DU-1227). Chem Pharm Bull 38: 529-531.
Ondetti MA. 1977. Design of specific inhibitors of angiotensinconverting enzyme: New class of orally active antihypertensive agents. Science 196: 441-444
Maruyama S, Mitachi H, Awaya J. 1987. Angiotensin I-converting enzyme inhibitory activity of the c-terminal hexapeptide of as l-casein. Agric Biol Chem 51: 2557-2561
Miyoshi S, Ishikawa I, Kaneko T, Fukui F, Tanaka H, Maruyama S. 1991. Structures and activity of angiotensinconverting enzyme inhibitors in an $\alpha$ -zein hydrolysate. Agric Biol Chem 55: 1313-1318
Chen JR, Okada T, Muramoto K. 2002. Identification of angiotensin I-converting enzyme inhibitory peptides derived from the peptic digest of soybean protein. J Food Biochem 6: 543-544
Astawan M, Wahyuni M, Yasuhara T. 1995. Effects of angiotensin I-converting enzyme inhibitory substances derived from Indonesian dried-salted fish on blood pressure of rats. Biosci Biotech Biochem 59: 524-529
Fujita H, Sasaki R, Yoshikawa M. 1995. Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine. Biosci Biotech Biochem 59: 2344-2345
Wako Y, Abe Y, Handa T, Ishikawa S. 1999. Angiotensin I-converting enzyme inhibitors in fish water soluble protein hydrolyzates prepared by bioreactor. Food Sci Technol Res 5: 378-380
Suetsuna K. 1998. Purification and identification of angiotensin l-converting enzyme inhibitors from the red alga Porphyra yezoensis. J Mar Biotech 6: 163-167
Suetsuna K, Nakano T. 2000. Identification of an antihypertensive peptide frompeptic digest of wakame (Undaria pinnatifida). J Nutr Biochem 11: 450-454
Lowry OH, Rosebrough NJ, Farr L, Rindall RJ. 1951. Protein mesurement with the folin phenol reagent. J Biol Chem 193: 256-259
Cushman DW, Chung HS. 1970. Spectrometric assay and properties of the angitensin I-converting enzyme of rabbit lung. Biochem Pharmaco 20: 1637-1684
Chandler SF, Dodds JH. 1993. The effect of phosphate, nitrogen and sucrose on the production phenolics and solasidine in callus cultures of Solanum laciniatum. Plant Cell Rep 2: 105-110
Adler-Nissen J. 1979. Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J Agric Food Chem 27: 1256-1262
Kim JM, Whang JH, Suh HJ. 2004. Enhancement of angitensin l-converting enzyme inhibitory activity and improvement of the emulsifying and foaming properties of com glutein hydrolysate using ultrafiltration membranes. Eur Food Res Technol 218: 133-138
Liu JC, Hsu FL, Tsai JC, Chan P, Liu JYH, Thomas GN, Tomlinson B, Lo MY, Lin JY. 2003. Antihypertensive effects of tannins isolated from traditional Chinese herbs as non-specific inhibitors of angiotensin converting enzyme. Life Sci 73: 1543-1555
Rojas A, Bah M, Rojas JI, Gutierrez DM. 2000. Smooth muscle relaxing activity of gentiopicroside isolated from Gentiana spathacea. Planta Med 66: 765-767
Black HR, Ming S, Poll DS, Wen YF, Zhou HY, Zhang ZQ, Chung YK, Wu YS. 1986. A comparison of the treatment of hypertension with Chinese herbal and Western medication. J Clin Hypertens 24: 371-378
Mao HY, Tu YS, Nei FD, Liang GF, Feng YB. 1981. Rapid antihypertensive effect of rhomotoxin in 105 hypertension cases. Chinese Med J 94: 733-736
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