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Effects of Lactobacillus delbrueckii...
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Ahmarani, Jamile.
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Effects of Lactobacillus delbrueckii ssp. lactis R0187 on soy flour fermentation.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Effects of Lactobacillus delbrueckii ssp. lactis R0187 on soy flour fermentation./
作者:
Ahmarani, Jamile.
面頁冊數:
87 p.
附註:
Source: Masters Abstracts International, Volume: 46-03, page: 1356.
Contained By:
Masters Abstracts International46-03.
標題:
Agriculture, Food Science and Technology. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=MR32650
ISBN:
9780494326503
Effects of Lactobacillus delbrueckii ssp. lactis R0187 on soy flour fermentation.
Ahmarani, Jamile.
Effects of Lactobacillus delbrueckii ssp. lactis R0187 on soy flour fermentation.
- 87 p.
Source: Masters Abstracts International, Volume: 46-03, page: 1356.
Thesis (M.Sc.)--McGill University (Canada), 2007.
Soy flour was inoculated with Lactobacillus delbrueckii ssp. lattis R0187, and incubated for 8 h, to evaluate the protein hydrolysis and identify peptides generated by this fermentation, and the impact on ACE and trypsin inhibitory activities. Aqueous protein extracts prepared from different fermentation time periods showed a decrease in soluble protein content (from 2.83 to 0.02 mg/mL), while soluble inorganic nitrogen and free amino acid contents increased (from 0.029 to 0.062% w/w, and from 0.75 to 0.90% w/w, respectively). The protein extracts were analyzed by SDS-PAGE; proteolysis was observed after 5 h incubation of inoculated soy flour, suggesting that glycinin, beta-conglycinin, and trypsin inhibitors, were hydrolyzed. Peptides were isolated by tricine-SDS-PAGE, and analyzed by MS/MS; fragments of soy anti-nutritional factors (Kunitz and Bowman-Birk trypsir, inhibitors), as well as of other soybean proteins, were identified, confirming that these proteins were hydrolyzed. The protein extracts at time 0 h and 8 h were analyzed by RP-HPLC; one fraction was analyzed by MS/MS, which identified peptides from Lactobacillus species. Determination of trypsin inhibitory activity showed less inhibition of the enzyme with inoculated soy flour compared to the control (un-inoculated soy flour), confirming the deactivation of trypsin inhibitors by fermentation. Determination of ACE inhibitory activity showed a higher inhibition with the control (86% +/- 3.0) compared to inoculated soy flour (66% +/- 7.6).
ISBN: 9780494326503Subjects--Topical Terms:
1017813
Agriculture, Food Science and Technology.
Effects of Lactobacillus delbrueckii ssp. lactis R0187 on soy flour fermentation.
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Soy flour was inoculated with Lactobacillus delbrueckii ssp. lattis R0187, and incubated for 8 h, to evaluate the protein hydrolysis and identify peptides generated by this fermentation, and the impact on ACE and trypsin inhibitory activities. Aqueous protein extracts prepared from different fermentation time periods showed a decrease in soluble protein content (from 2.83 to 0.02 mg/mL), while soluble inorganic nitrogen and free amino acid contents increased (from 0.029 to 0.062% w/w, and from 0.75 to 0.90% w/w, respectively). The protein extracts were analyzed by SDS-PAGE; proteolysis was observed after 5 h incubation of inoculated soy flour, suggesting that glycinin, beta-conglycinin, and trypsin inhibitors, were hydrolyzed. Peptides were isolated by tricine-SDS-PAGE, and analyzed by MS/MS; fragments of soy anti-nutritional factors (Kunitz and Bowman-Birk trypsir, inhibitors), as well as of other soybean proteins, were identified, confirming that these proteins were hydrolyzed. The protein extracts at time 0 h and 8 h were analyzed by RP-HPLC; one fraction was analyzed by MS/MS, which identified peptides from Lactobacillus species. Determination of trypsin inhibitory activity showed less inhibition of the enzyme with inoculated soy flour compared to the control (un-inoculated soy flour), confirming the deactivation of trypsin inhibitors by fermentation. Determination of ACE inhibitory activity showed a higher inhibition with the control (86% +/- 3.0) compared to inoculated soy flour (66% +/- 7.6).
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