| Summary: | 碩士 === 國立臺灣海洋大學 === 食品科學系 === 99 === The domestic cultivated Chlorella sorokiniana as a material , the inhibitory effects of α-glucosidase and α-amylase of Chlorella sorokiniana hydrolysates (hydrolyzed by cellulase and protease) were investigated, and purified bioactive substances from hydrolysate having the highest α-glucosidase and α-amylase inhibitory activity to evalvate the physiological effect on regulation of blood sugar. When adding 5% cellulase and 2% protease in the Chlorella hydrolysates (pulverized cell), hydrolysed for 3 h, the soluble protein, carbohydrate, and total polyphenol contents was 641、227 and 25 mg/g, repectively. To explore glycosidase inhibition from different sources, the hydrolysate had better inhibition on yeast from (Saccharomyces cerevisiae) (IC50＝26.5 mg/mL), but on α-amylase from porcine pancreas, (IC50＝14.3 mg/mL). Then, the hydrolysate (pulverized cell) was separated into five fractions by size exclusion chromatography on a Sephadex-15 column. The C2 fraction (M.W.=370-280Da) of the hydrolysate showed the lowest α-glucosidase IC50 being 3.23 mg /mL. The C2 fraction was further analyzed by HPLC, only peak C2-1 had inhibitory effect on α-glucosidase and its IER was 542.9 %/mg/mL.
The muscle of freshwater clam was extracted using hot water. The residual muscle was freeze dried then hydrolyzed by Protamex (PX) for 5 hr, the soluble protein, peptide, and carbohydrate contents was 596、160 and 360 mg/g, repectively. The inhibitory effects of freshwater clam hydrolysates (hydrolyzed by Protamex) on activity of α-glucosidase and α-amylase were investigated. The sources of the yeast AG and porcine pancreas AA had ad the higest α-glucosidase and α-amylase inhibitory activity (IC50＝14.6 and 11.9 mg/mL), repectively.
|
|---|
