한국식품영양과학회지 (Journal of the Korean Society of Food Science and Nutrition)

  • 제37권12호
  • /
  • Pages.1548-1553
  • /
  • 2008
  • /
  • 1226-3311(pISSN)
  • /
  • 2288-5978(eISSN)
한국식품영양과학회 (The Korean Society of Food Science and Nutrition)
권호 표지
DOI QR코드

DOI QR Code

한천 유기산 가수분해물의 생리활성

Functional Properties of Hydrolysates Prepared from Agar Treated with Organic Acids

  • 주동식 (한중대학교 외식산업학과) ;
  • 이창호 (강릉대학교 생물학과) ;
  • 조순영 (강릉대학교 동해안해양생물자원연구센터)
  • Joo, Dong-Sik (Dept. of Foodservice Industry, Hanzhong University) ;
  • Lee, Chang-Ho (Dept. of Biology, Kangnung National University) ;
  • Cho, Soon-Yeong (East Coastal Marine Bioresources Research Center, Kangnung National University)
  • 발행 : 2008.12.31
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

한천 가수분해물의 각종 생리활성을 실험한 결과, $100^{\circ}C$ 이상의 조건에서 가수분해된 시료에서 B. cereus와 B. subtilis에 강한 항균활성을 나타내었는데 특히, malate 가수분해물에서 활성이 높은 것으로 나타났으며, 일부 획분에서는 E. coli에 대해서도 확실한 항균 효과를 나타내었고, 약하지 만 S. aureus에 대해서도 항균활성을 나타내었다. Citrate와 malate로 가수분해된 시료에서 $55{\sim}80%$의 tyrosinase 활성을 저해하는 것으로 나타났으나 전체적으로 활성이 낮았다. 한천 가수분해물의 비피더스균 증식 효과는 온도에 관계없 이 lactate, citrate 및 malate로 가수분해된 시료에서 B. infantis 균에 대해 증식효과가 확인되었다. 한천 가수분해물에서는 ACE 저해능이 확인되지 않았으며, 항혈액응고활성도 거의 나타나지 않았다. 한편, 세포증식 억제능은 0.5%의 citrate와 lactate로 $110^{\circ}C$에서 180분간 가수분해되어진 시료에서 강한 활성이 확인되었으며, 이들 시료를 정제하여 얻어진 특정 획분(C3과 L3)에서도 강한 세포 증식 억제능이 확인되었다.

This study was concerning various physiological activities of agar hydrolysates. All agar hydrolysates showed strong antimicrobial activity against Bacillus subtilis and Bacillus cereus. Also, the agar hydrolysates prepared at the temperature of $110^{\circ}C$ or $120^{\circ}C$ showed antimicrobial activity against St. aureus and E. coli. Among the agar hydrolysates, several hydrolysates treated with citrate or malate at $110^{\circ}C$ or $120^{\circ}C$ conditions showed tyrosinase activity inhibition, and their inhibition rates of tyrosinase activity were about 80%. Some tested samples treated with 0.5% organic acid at $100^{\circ}C$ or $110^{\circ}C$ inhibited the growth of cancer cell. Two agar hydrolysates prepared with 0.5% citrate and lactate at $110^{\circ}C$ for $180^{\circ}C$ min had relatively high cancer cell growth inhibition among the tested samples. The agar hydrolysates treated with citrate and lactate at $110^{\circ}C$ for 180 min obtained the main peaks of six and seven from Sephadex G-15 column chromatography. Among the main peaks, the cancer cell growth inhibition of C-3 and L-3 fractions were higher than that of other fractions.

키워드

참고문헌

  1. Alonso S, Setser C. 1994. Functional replacements for sugars in foods. Trends Food Sci Techonol 5: 139-146 https://doi.org/10.1016/0924-2244(94)90119-8
  2. Araki CL. 1965. Some recent studies on the polysaccharides of agarophytes. In Proc. Int. Seaweed Symp. 5. Young EG, Maclahan JL, eds. Pergamon Press, London. p 3-17
  3. Durkworth M, Yaphe W. 1970. Thin-layer chromatographic analysis of enzymic hydrolysates of agar. J Chrom 49: 482-487 https://doi.org/10.1016/S0021-9673(00)93663-X
  4. Harris P. 1990. Food gels. Elsevier Applied Science, London. p 1-34
  5. Kato I. 1999. The functions of agar and agarooligosaccharides. Food & Develop 33: 44-46
  6. Groleau D, Yaphe W. 1977. Enzymatic hydrolysis of agar; purification and characterization of ${\bata}$-neoagarotetraose hydrolase from Pseudomonas atlantica. Can J Microbiol 23: 672-679 https://doi.org/10.1139/m77-100
  7. Joo DS, Cho SY, Lee EH. 1998. Preparation of agar hydrolysates by agarase and functionality of the hydrolysates. Korean J Biotechnol Bioeng 13: 378-382
  8. Joo DS, Kim OS, Cho SY, Lee CH. 2003. Preparation conditions of agarooligosaccharides with organic acids. J Korean Fish Soc 36: 6-10
  9. Somogyi M. 1952. Notes on sugar determination. J Biol Chem 195: 19-23
  10. Dubois M, Gilles KA, Hamilton JK, Rebers PA, Smith F. 1956. Colorimetric method for determination of sugar and related substances. Anal Chem 28: 350-356 https://doi.org/10.1021/ac60111a017
  11. Lorian V. 1991. Antibiotics laboratory medicine. Williams & Wilkins, Baltimore. p 17-105
  12. Teraguchi S, Uehara M, Ogasa K, Mitsuoka T. 1978. Enumeration of bifidobacteria in dairy products. Jpn J Bacterial 33: 753-758 https://doi.org/10.3412/jsb.33.753
  13. Horowitz NH, Fling M, Macleod HA, Sheoka N. 1960. Genetic determination and enzymatic induction of tyrosinase in Neurospora. J Mol Biol 2: 96-104 https://doi.org/10.1016/S0022-2836(60)80031-9
  14. Cushman DW, Cheung HS. 1971. Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Bichim Pharmacol 20: 1637-1648 https://doi.org/10.1016/0006-2952(71)90292-9
  15. Nishimo T, Nagumo T. 1992. Anticoagulant and antithrombin activities of oversulfated fucans. Carbohydr Res 229: 355-362 https://doi.org/10.1016/S0008-6215(00)90581-0
  16. Bullen CL, Teale PV, Willis AT. 1976. Bifidobacteria in the intestinal tract on infants. An in vivo study. J Med Microbiol 3: 338-344
  17. Marayama S, Mitachi H, Tanaka H, Tomizuka N, Suzuki H. 1987. Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein. Agric Biol Chem 51: 1581-1586 https://doi.org/10.1271/bbb1961.51.1581
  18. Hirata A, Itoh W, Tabata K, Kojima T, Itoyama S, Sugawara I. 1994. Anticoagulant activity of sulfated schizophyllan. Biosci Biotech Biochem 58: 406-407 https://doi.org/10.1271/bbb.58.406