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Production and Purification of Bioactive Peptides from Fermented Hydrolysate of Chlorella
|Authors: ||Kuan-Ting Pei|
|Contributors: ||NTOU:Department of Food Science|
|Issue Date: ||2011-06-30T08:17:56Z
|Abstract: ||以破胞綠藻為原料，探討同時發酵水解與先水解再發酵對其水解物抑制血管升壓素轉換酶(Angiotensin I-converting enzyme, ACE)活性與γ-胺基丁酸(γ-aminobutyric acid, GABA)產量的影響。綠藻先水解再發酵者，其對ACE的IC50值由0.08增加至0.10 mg peptide/mL。但GABA可由104.6增至117.1 mg/100g。此樣品經由腸胃道消化作用後其IC50值由0.10增加至0.12 mg peptide/mL。發酵水解物經由Sephadex G-15的膠體層析可得四個劃分物，其中以第四劃分物(D)的分子量360-330 Da有最低的IC50值，為0.0029 mg peptide/ mL。劃分物D再經由高效能液相層析法(C18管柱)分離，可得五個尖峰物質。其中以D2有最高之IER值，為為474 %/μg/ mL。|
The pulverized Chlorella was the experimental material. The differences between the hydrolysis fermentation and the fermentation after followed hydrolysis on the inhibitory effect of the supernatant against angiotensin I-converting enzyme (ACE) and production of γ-aminobutyric acid (GABA) were investigated. The ACE IC50 of the supernatant fermented-after-hydrolyzed increased from 0.08 to 0.10 mg peptide/mL, and the content of GABA increased from 104.6 to 117.1 mg/100g. Then, the fermented after hydrolyzed supernatant was digested by gastrointestinal proteases. After digestion, the ACE IC50 was increased from 0.10 to 0.12 mg peptide/mL. The supernatant was separated into four fractions (A-D) by size exclusion chromatography on a Sephadex G-15 column. The fourth fraction of supernatant having molecular weight ranged 360-330 Da showed the lowest IC50 being 2.9 μg peptide/ mL. This fraction was further analyzed by HPLC (C18 column) and separated into five peaks. The peak D2 had the most active peptides and the highest IER value being 474 %/μg/ mL.
|Appears in Collections:||[食品科學系] 博碩士論文|
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