Inhibition of α-Glucosidase and α-Amylase from the Hydrolysate of Laminaria japonica / 海帶水解物對 α-葡萄糖苷酶與 α-澱粉酶之抑制效果

碩士 / 國立臺灣海洋大學 / 食品科學系 / 99 / The inhibitory effect of Laminaria hydrolysates (hydrolyzed by cellulase and protease) and fermented hydrolysates (fermented with mixed lactic acid bacteria) on α-glucosidase and α-amylase ,and in vitro of bile acid binding capacity were investigated. The yield of hydrolysate increased from 21.4 to 37.8%, as adding 5 or 10% cellulase and 2% protease in the Laminaria. The total carbohydrate and peptide content of Laminaria hydrolysates were increased from 229.4 to 418.9 mg/g and from 5.3 to 88.7 mg/g, respectively, as the hydrolysis time from 3 to 9 h. The inhibition of hydrolysate (hydrolysis for 3 h) on α-glucosidase and α-amylase IC50 were 17.0 and 45.4 mg/mL, respectively. This hydrolysate was separated by ultrafiltration using 5000 Da membranes, and its α-glucosidase IC50 was 10.4 mg/mL. The yield of hydrolysates was increased from 30.1 to 58.4%, and total carbohydrate content was increased from 340.4 to 400.6 mg/g. The fermented hydrolysate on α-glucosidase and α-amylase IC50 were 22.4 and 29.8 mg/mL, respectively. This hydrolysate was separated into two fractions by size exclusion chromatography on a Sephadex-15 column. The second fraction showed the highest α-glucosidase inhibitory efficiency ratio (IER) as base on carbohydrate and peptide compound being 7.2 and 45.3 %/mg/mL. The bile acid binding capacity of Laminaria powder (whole Laminaria, hydrolysates residue and fermented hydrolysates residue) were 9.7, 11.7 and 10.7%, respectively, as compared to cholestyramine.

Identiferoai:union.ndltd.org:TW/099NTOU5253010
Date January 2011
CreatorsChiung-Chieh Chang, 張瓊潔
ContributorsJenn-Shou Tsai, 蔡震壽
Source SetsNational Digital Library of Theses and Dissertations in Taiwan
Languagezh-TW
Detected LanguageEnglish
Type學位論文 ; thesis
Format79

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