• Journal of Ginseng Research
• /
• v.20 no.3
• /
• pp.248-255
• /
• 1996

This study was devised to observe in vitro, the inhibitory effects of acidic polysaccharide fractions from Korean red ginseng (KRG) and white ginseng (KWG) on the lipolytic action of loxohormone-L and on angiotensin converting enzyme (ACE, peptidyldipeptidase hydrolase, EC 3.4.15.1) . The crude acidic polysaccharides (CAP) extracted from main and lateral roots of KRG and KWG were separately purified through several procedures. The total inhibitory activities on the lipolytic action of toxohormone-L of CAP from main roots of KRG and KWG was higher than those of CAP from lateral roots of KRG and KWG, respectively, and that of CAP from main root of KRG was 3.1 times higher than that of CAP from main root of KWG. The specific activity of CAP from main root of KRG was measured as 5.40 units/mg, when one unit was defined as the amount giving 50% inhibition on toxohormone-L induced lipolysls. A subfraction named PG4 3 obtained by replanted chromatography on DEAE-TOYOPEARL 650M gave the specific activity of 24.4 units/mg. On the other hand, it was found that the total inhibitory activity on ACE of CAP from lateral root of KRG was the highest among the 4 kinds of CAP, but the specific activity of CAP from lateral root of KWG was the highest.

• Korean Journal of Food Science and Technology
• /
• v.29 no.6
• /
• pp.1316-1318
• /
• 1997

The isolated ${\kappa}-Casein$ on gel permeation chromatography was hydrolyzed by chymosin, trypsin, and pepsin. The 3% TCA soluble portion of the hydrolysates were dialyzed on the angiotensin-I converting enzyme (ACE) inhibition rate (%,) and inhibitory activity $(IC_{50})$ were determined. The trypsin hydrolysate exhibited the highest ACE inhibition rate while the chymosin hydrolysation showed the lowest activity. The hydrolysate was dialyzed using dialysis membrane with various molecular cut-offs, and $IC_{50}$ was determined. As the pore size of the dialysis tubing increased, the ACE inhibitory activity decreased.

• Food Science of Animal Resources
• /
• v.42 no.1
• /
• pp.46-60
• /
• 2022

In this study, angiotensin-I-converting enzyme inhibitory (ACEI) activity was evaluated in fermented goat milk fermented by lactic acid bacteria (LAB) from fermented foods and breast milk. Furthermore, the potential for ACEI peptides was identified in fermented goat milk with the highest ACEI activity. The proteolytic specificity of LAB was also evaluated. The 2% isolate was inoculated into reconstituted goat milk (11%, w/v), then incubated at 37℃ until pH 4.6 was reached. The supernatant produced by centrifugation was analyzed for ACEI activity and total peptide. Viable cell counts of LAB and titratable acidity were also evaluated after fermentation. Peptide identification was carried out using nano liquid chromatography mass spectrometry (LC-MS/MS), and potential as an ACEI peptide was carried out based on a literature review. The result revealed that ACEI activity was produced in all samples (20.44%-60.33%). Fermented goat milk of Lc. lactis ssp. lactis BD17 produced the highest ACEI activity (60.33%; IC₅₀ 0.297±0.10 mg/mL) after 48 h incubation, viable cell counts >8 Log CFU/mL, and peptide content of 4.037±0.27/mL. A total of 261 peptides were released, predominantly derived from casein (93%). The proteolytic specificity of Lc. lactis ssp. lactis BD17 through cleavage on the amino acid tyrosine, leucine, glutamic acid, and proline. A total of 21 peptides were identified as ACEI peptides. This study showed that one of the isolates from fermented food, namely Lc. lactis ssp. lactis BD17, has the potential as a starter culture for the production of fermented goat milk which has functional properties as a source of antihypertensive peptides.

• Proceedings of the PSK Conference
• /
• 2003.04a
• /
• pp.226.3-227
• /
• 2003

Lactic acid bacteria have been considered as the most beneficial probiotic organisms contributing to inhibition of harmful and putrefactive intestinal bacteria. Among them, Bifidobacterium spp. has been considered as one of the most beneficial probiotic organism that can improve the health of humans, since it is one of the major bacteria flora in human intestine. However, the harmful enzyme-inhibitory activity of lactic acid bacteria of Kimchi, which is a representative Korean fermented food has not been evaluated. (omitted)

• Bulletin of the Korean Chemical Society
• /
• v.23 no.4
• /
• pp.593-597
• /
• 2002

(R,S)- and (R)-2-Benzylcysteine (1) and (R,S)-2-phenethylcysteine (2) were synthesized and evaluated as inhibitors for carboxypeptidase A (CPA) with the expectation that these compounds exhibit improved inhibitory activities over 2-benzyl-3-mercaptopropanoic acid (BMPA), a potent CPA competitive inhibitor, possibly having additional interactions of their amino group with the carboxylate of Glu-270 of the enzyme upon binding to CPA. Contrary to the expectation, however, the CPA inhibitory potencies of these compounds were found to be much reduced compared with that of BMPA, suggesting that the amino group in the inhibitors rather exerts steric hindrance in binding of these inhibitors to CPA.

• Archives of Pharmacal Research
• /
• v.26 no.9
• /
• pp.735-738
• /
• 2003

The methanolic extract of the twigs of Celtis chinensis was found to show inhibitory activity on acetylcholinesterase (AChE), an enzyme that plays a role in the metabolic hydrolysis of ACh. Bioassay-guided fractionation of the methanolic extract resulted in the isolation of N-p-coumaroyl tyramine. as an inhibitor on AChE. This compound inhibited AChE activity in a dose-dependent manner, and the $IC_50$ value of trans-N-p-coumaroyl tyramine was 34.5 $\mu$g/mL (122 $\mu$M).

• Bulletin of the Korean Chemical Society
• /
• v.27 no.9
• /
• pp.1353-1358
• /
• 2006

We investigated in vitro T-cell inhibitory activity and bioavailability of small chemical inhibitors for Lck SH2 domain, which had a different scaffold such as an amide bond, reduced amide bond, N-methyl amide bond, thioamide bond, and urethane bond. Each of these compounds, with its particular scaffold, showed a different logP value, stability against serum enzyme, stability in buffer solution, and in vitro T-cell inhibitory activity. Overall results indicated that the SH2 inhibitor containing urethane bond can be a new lead compound because of its superior bioavailability, potent in vitro T-cell inhibitory activity, and facile synthesis.

• YAKHAK HOEJI
• /
• v.46 no.6
• /
• pp.387-391
• /
• 2002

In vitro $\beta$-lactamase inhibitory activity of 6-exomethylene sulbactam compounds (CH-120, 130, 140, 145, 150, 155) was compared with clavulanic acid, sulbactam and tazobactam. The inhibitory activity of CH-140 was stronger than sulbactam and clavulanic acid against Type II, III, IV, TEM enzymes and stronger than tazobactam against Type IV enzyme. The inhibitory activity of CH-145 was stronger than sulbactam and clavulanic acid against Type I, II, III, IV, TEM enzymes and stronger than tazobactam against Type III, IV enzymes. The in vitro antimicrobial activity of CH-140 and CH-145 combined with piperacillin and ceftriaxone was compared with the sulbactam and tazobactam against $\beta$-lactamase producing 31 strains. But, synergistic activity of CH-140 and CH-145 was inferior to tazobactam.

• Korean Journal of Pharmacognosy
• /
• v.45 no.4
• /
• pp.359-365
• /
• 2014

Aldose reductase (AR) is the key enzyme of the polyol pathway in the development of the diabetic complications. Sixty seven Chinese herbal medicines have been investigated for inhibitory activities on AR. Among them, 7 herbal medicines, Buddleja crispa (twigs and leaves), Taiwania flousiana (twigs and leaves), Sloanea hemsleyana (fruits), Euphorbia nemetocypha (whole plants), Photinia glomerata (twigs and leaves), Vitex yunnanensis (twigs and leaves) exhibited a significant inhibitory activity against AR. Particularly, S. hemsleyana and V. yunnanensis showed 1.2-4.5 times more potent inhibitory activity than the positive control, 3,3-tetramethyleneglutaric acid (TMG).

• Natural Product Sciences
• /
• v.6 no.1
• /
• pp.36-39
• /
• 2000

Acorenone, a diterpene isolated from Acorus gramineus, showed strong resistance inhibitory activity against multi-drug resistant microorganisms such as Staphylococcus aureus SA2, which has resistance to 10 usual antibiotics including chloramphenicol (Cm). At the level of $5\;{\mu}g/ml$ when combined with $50\;{\mu}g/ml$ of Cm. Bacterial resistance to Cm is due to the presence in resistant bacteria of an enzyme, chloramphenicol acetyltransferase (CAT), which catalyses the acetyl-CoA dependent acetylation of the antibiotic at C-3 hydroxyl group. To elucidate the mechanism of resistant inhibitory effect, the acorenone which had the strongest resistant inhibitory activity, was investigated on the CAT assay. As the result, the combination of Cm and acorenone showed the strongest inhibitory activity on CAT as noncompetitive and dose dependent manner.