Abstract: Fecal sterol has been proposed as a chemical indicator
of human fecal pollution even when fecal coliform populations have
diminished due to water chlorination or toxic effects of industrial
effluents. This paper describes an improved derivatization procedure
for simultaneous determination of four fecal sterols including
coprostanol, epicholestanol, cholesterol and cholestanol using gas
chromatography-mass spectrometry (GC-MS), via optimization study
on silylation procedures using N-O-bis
(trimethylsilyl)-trifluoroacetamide (BSTFA), and
N-(tert-butyldimethylsilyl)-N-methyltrifluoroacetamide
(MTBSTFA), which lead to the formation of trimethylsilyl (TMS) and
tert-butyldimethylsilyl (TBS) derivatives, respectively. Two
derivatization processes of injection-port derivatization and water bath
derivatization (60 oC, 1h) were inspected and compared. Furthermore,
the methylation procedure at 25 oC for 2h with
trimethylsilydiazomethane (TMSD) for fecal sterols analysis was also
studied. It was found that most of TMS derivatives demonstrated the
highest sensitivities, followed by methylated derivatives. For BSTFA
or MTBSTFA derivatization processes, the simple injection-port
derivatization process could achieve the same efficiency as that in the
tedious water bath derivatization procedure.
Abstract: Biologically active peptides are of particular interest
in food science and human nutrition because they have been shown to play several physiological roles. In vitro gastrointestinal digestion of lentil and whey proteins in this study produced high angiotensin-I converting enzyme inhibitory activity with 75.5±1.9 and 91.4±2.3%
inhibition, respectively. High ACE inhibitory activity was observed in lentil after 5 days of germination (84.3±1.2%). Fractionation by
reverse phase chromatography gave inhibitory activities as high as
86.3±2.0 for lentil, 94.8±1.8% for whey and 93.7±1.7% at 5th day of germination. Further purification by HPLC resulted in several
inhibitory peptides with IC50 values ranging from 0.064 to 0.164
mg/ml. These results demonstrate that lentil proteins are a good
source of peptides with ACE inhibitory activity that can be released by germination or gastrointestinal digestion. Despite the lower bioactivity in comparison with whey proteins, incorporation of lentil proteins in functional food formulations and natural drugs look promising.