• Preventive Nutrition and Food Science
• /
• v.19 no.1
• /
• pp.5-9
• /
• 2014

This study was designed to investigate the inhibitory effects of Polyopes lancifolia extract (PLE) on ${\alpha}$-glucosidase activity, ${\alpha}$-amylase activitiy, and postprandial hyperglycemia in streptozotocin (STZ)-induced diabetic mice. The results of this study revealed a marked inhibitory effect of PLE on ${\alpha}$-glucosidase and ${\alpha}$-amylase activities. The $IC_{50}s$ of PLE against ${\alpha}$-glucosidase and ${\alpha}$-amylase were 0.20 mg/mL and 0.35 mg/mL, respectively. PLE was a more effective inhibitor of ${\alpha}$-glucosidase and ${\alpha}$-amylase activities than acarbose, the positive control. The postprandial blood glucose levels of STZ-induced diabetic mice were significantly lower in the PLE treated group than in the control group. Moreover, PLE administration was associated with a decreased area under the curve for the glucose response in diabetic mice. These results indicate that PLE may be a potent inhibitor of ${\alpha}$-glucosidase and ${\alpha}$-amylase activities and may suppress postprandial hyperglycemia.

• Food Science and Preservation
• /
• v.22 no.3
• /
• pp.345-352
• /
• 2015

This study was monitored the quality characteristic of the hyssop-rice drink added using hyssop (Hyssopus officinalis) and rice. AFter operational parameters including amylase content ($X_1$, 1~5 mL), saccharification time ($X_2$, 10~18 hr) and hyssop content ($X_3$, 1.0~3.0 g) were monitored, these results were analyzed using a response surface methodology for the determination of the optimum conditions (Brix, Hunter's color and organoleptic properties). Maximum conditions of Brix for the hyssop-rice drink were 0.96 mL of amylase, 14.93 hr of saccharification time and 2 g of hyssop. Maximum conditions of Hunter's color b were 1.90 mL of amylase, 16.64 hr of saccharification time and 2.51 g of hyssop. Maximum conditions of organoleptic color were 4.60 mL of amylase, 15.66 hr of saccharification time and 1.57 g of hyssop. Maximum conditions of organoleptic aroma were 3.46 mL of amylase, 10.79 hr of saccharification time and 1.45 g of hyssop. Maximum conditions of organoleptic taste were 3.67 mL of amylase, 17.64 hr of saccharification time and 1.76 g of hyssop. Maximum conditions of overall palatability of the hyssop-rice drink were 3.73 mL of amylase, 13.66 hr of saccharification time and 1.85 g of hyssop.

• Journal of Sericultural and Entomological Science
• /
• v.16 no.1
• /
• pp.57-65
• /
• 1974

This study has been carried out to investigate the effect of protein components of a diet on the increasing of larval body weight and diet efficiency, as well as the amylase activity of larval digestive juices during the 5th instar. Defending on the amounts of soybean meal as a protein source, the six different kind of artificial diets containing mulberry leaf powder fed to the larvae. The results obtained may be summarized as follows： 1. As the protein components of the diet were increased, the amount of increased larval body weight was also increased. 2. As the protein components of the diet were increased, both the cocoon weight and cocoon layer weight were also increased. 3. As the protein components of the diet were increased, both the amount of diet digested and coefficient of digestibility were also increased. 4. As the protein components of the diet were increased, the diet efficiency of larvae were also increased. 5. But the experimenters could not observe any correlation between the increase of protein components of a diet and the amylase activity of the digestive juices.

• Korean Journal of Food Science and Technology
• /
• v.17 no.4
• /
• pp.240-244
• /
• 1985

Curde $\beta$-amylase was prepared by frationation of the water extracts from Korean ginseng, Panax Ginseng C.A. Meyer, with 0.2-0.6 saturation of ammonium sulfate. The enzyme showed the typical properties of $\beta$-amylase, producing only maltase from starch. The enzyme preparation also showed no maltase activity. The enzyme was stable at the pH 5-9 and at the temperature below $40^{\circ}C$. The enzyme showed the optimum pH at 5.0 and the optimum temperature at $35^{\circ}C$. Its activities had proportional relations with substrate concentration below 12 mg%, showing Km V slues of 4.76 mg%. The enzyme was inhibited by $Ag^{+}$, $Hg^{++}$, $Cd^{++}$, $Cu^{++}$,$ Al^{3+}$, and $Fe^{3+}$.

• KOREAN JOURNAL OF CROP SCIENCE
• /
• v.41 no.5
• /
• pp.542-550
• /
• 1996

An experiment with alfalfa (Medicago sativa L.) plants was designed to investigate the changes in non-structural carbohydrate (NSC) contents and the activities of amylolytic enzymes during a regrowth period following defoliation. Sampling from hydroponic grown-plants were carried out at intervals during 24 days of regrowth. Shoot regrowth was very slow during the first 10 days and root growth was depressed after defoliation. Defoliation induced a great decrease in both total sugar and starch contents in taproots during the first 10∼14 days. A major recovery of NSC occurred from day 15. Averaged over sampling dates, the activity of exo-amylase was about 400-fold higher than that of endo-amylase. Exo-amylase activity in defoliate plants slightly increased until day 6 (maximum level) and then decreased. Endo-amylase rapidly increased for the first 4 days after defoliation and slightly increased afterwards to a maximum on day 24. These results showed that increase in amylolytic enzyme activity in taproots coincided with the time of starch utilization during regrowth and that indicated it plays an important role in starch degradation.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.19 no.6
• /
• pp.625-635
• /
• 1990

The purpose of this study was focused on investigation of biochemical properties of amylases in germinating corn(Zea mays L.) the amylase(I), (II) and (III) from germinating corn seeds were partially purified by ammonium sulfate precipitation, DEAE-Sephadex A-50 ion exchange column chromatography and Sephadex G-100 gel filtration. The last step was effective for separation of the corn amylases to a homogeneous slate. the purified amylase(I) was identified as a kind of $\alpha$-amylase from the fact that 5％ starch solution was hydrolysed into mainly maltose and maltotetrose by it, and amylase(II) and amylase(III) were enzymes producing maltotetrose as main product. The molecular weight and specific activity of the amylase(I), (II) and (III) were determined to be 54,000 and 70.47 unit/mg, 39,000 and 62.98 unit/mg, and 51,000 and 80.39 unit/mg, respectively. It showed a tendency to increase the amylases activities in presence of Ba, Ca, Co and Fe groups, but inhibits in that of Ag, Sn, Hg and Zn groups, and amylase(I), (II) and (III) remained stable at pH 5-6 and 2$0^{\circ}C$ for 40 days in containing of 1 mM CaCl$_2$. The optimum pH and optimum temperatures were pH 6, pH 5 and pH 6 and 35$^{\circ}C$, 55$^{\circ}C$ and 55$^{\circ}C$, respectively. These results suggest that the amylase(I), (II) and (III) were different amylases.

• Journal of Microbiology and Biotechnology
• /
• v.14 no.6
• /
• pp.1196-1199
• /
• 2004

A bacterium, isolated from rabbit's waste and identified as Cellulomonas sp., had cellulase and thermostable $\alpha$-amylase activity when grown on wheat bran. Maximum activity of thermostable $\alpha$-amylase was obtained by adding $3\%$ soluble starch. However, soybean oil (1 ml $1^{-1}$) could increase the production of $\alpha$-amylase and cellulase in 'wheat bran. The $\alpha$-amylase was characterized by making a . demonstration of optimum activity at $90^{\circ}C$ and pH 6- 9, with soluble starch as a substrate. The effect of ions on the activity and the stability of this enzyme were investigated. This strain secreted carboxymethyl cellulase (CMCase), cellobiase ($\beta$­glucosidase), and filter paperase (Fpase) during growth on wheat bran. Carboxymethy1cellulase, cellobiase, and Fpase activities had pH optima of 6, 5.5, and 6, respectively. CMCase and cellobiase activities both had an optimum temperature of $50^{\circ}C$, whereas Fpase had an optimum temperature of $45^{\circ}C$.

• Mycobiology
• /
• v.29 no.4
• /
• pp.183-189
• /
• 2001

Extracellular amylase properties were examined with the mycelium of Tricholoma matsutake isolated from ectomycorrhizal roots of Pinus densiflora. The molecular weights of $\alpha$-amylase and glucoamylase were estimated as 34.2 kD and 11.5 kD, respectively, after eluted through Superdex 75 column. The optimum pH of the purified enzyme was found in a range of pH $5.0{\sim}6.0$, with a peak at pH 5.0. The activities of these enzymes were stable from $4^{\circ}C\;to\;30^{\circ}C$. The $\alpha$-amylase of T. matsutake readily hydrolyzed soluble starch and amylose-B, while it weakly hydrolyzed glycogen, dextrin, amylose and amylose-A. The main products of hydrolysis were confirmed to be glucose, maltose and maltotriose on the basis of the similarities in the thin layer chromatographic mobility.

• BMB Reports
• /
• v.40 no.4
• /
• pp.494-500
• /
• 2007

The endophytic bruchid pest Callosobruchus maculatus causes severe damage to storage cowpea seeds, leading to economical losses. For this reason the use of $\alpha$-amylase inhibitors to interfere with the pest digestion process has been an interesting alternative to control bruchids. With this aim, $\alpha$-amylase inhibitors from baru seeds (Dipteryx alata) were isolated by affinity chromatographic procedures, causing enhanced inhibition of C. maculatus and Anthonomus grandis $\alpha$-amylases. To attempt further purification, this fraction was applied onto a reversed-phase HPLC column, generating four peaks with remarkable inhibition toward C. maculatus $\alpha$-amylases. SDS-PAGE and MALDI-ToF analysis identified major proteins of approximately 5.0, 11.0, 20.0 and 55 kDa that showed $\alpha$-amylase inhibition. Results of in vivo bioassays using artificial seeds containing 1.0% (w/w) of baru crude extract revealed 40% cowpea weevil larvae mortality. These results provide evidence that several $\alpha$-amylase inhibitors classes, with biotechnological potential, can be isolated from a single plant species.

• The Korean Journal of Mycology
• /
• v.17 no.3
• /
• pp.149-153
• /
• 1989

One strain of Aspergillus niger K-25 producing an acid-stable ${\alpha}-amylase$ was isolated from the soil. The optimum culture conditions were investigated. The production of the acid-stable ${\alpha}-amylase$ was enhanced when the strain was incubated in a medium containing soluble starch 3.5%, peptone 2%, $KH_2PO_4$ 0.5%, $MaSO_4{\cdot}7H_2O$ 0.25% and $FeCI_3$ 1.0% at pH 3 for 7 days. However, higher activity of acid-stable ${\alpha}-amylase$ was demonstrated on wheat bran culture. Amylase production was doubled when A. niger K-25 was incubated on the wheat bran supplemented with fumaric acid buffer (pH 3).