• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.2
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• pp.163-167
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• 2010

[ $\alpha$ ]Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, $\alpha$-glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose, sucrose, trehalose, and p-nitrophenyl $\alpha$-D-glucopyranoside as substrates. In general, hemolymph $\alpha$-glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut $\alpha$-glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. $\alpha$-Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl $\alpha$-D-glucoside (MUG) indicated that the $\alpha$-glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to $\alpha$-glucosidase activity from A. yamamai, $\alpha$-glucosidase activity from B. mori was generally less sensitive to the $\alpha$-glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose, sucrose, and trehalose.

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.427-429
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• 1996

We have already cloned an extracellular $\alpha$-glucosidase gene from Aspergillus niger with oligonucleotide probe synthesized on the basis of the peptide sequences determined previously. The DNA sequence revealed an open reading frame of 895 amino acids split by three introns. We are attempting to construct an A. niger strain deficient in the $\alpha$-glucosidase enzyme activity, which would be useful for the glucoamylase production without contamination by the industrially undesirable $\alpha$-glucosidase. For destruction of the $\alpha$-glucosidase gene, we try to make transformations. A cloned partial $\alpha$-glucosidase gene was introduced into Aspergillus niger, and transformants with suppressed $\alpha$-glucosidase activity were isolated. The transformants were cultured on YPD medium which contained Hygromycin B at 30$\circ$C. The activity of $\alpha$-glucosidase of the suppressed transformants was compared to that of wild type activity. As shown by southern-hybridization, we detected that the transformant was a heterocaryon.

• Food Engineering Progress
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• v.14 no.3
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• pp.243-248
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• 2010

The ${\beta}$-glucosidase (E.C. 3.2.1.21) production capabilities of lactic acid bacteria isolated from a variety of kimchi (fermented vegetables) were examined. When grown in a medium containing cellobiose as carbon source, most lactic acid bacteria showed significantly higher intracellular levels of ${\beta}$-glucosidase than the extracellular levels. A maximum intracellular ${\beta}$-glucosidase activity of 3.7${\pm}$0.5 (unit/mg protein) was obtained in the case of Weissella cibaria KFRI88010 isolated from kimchi. The optimum reaction conditions for W. cibaria KFRI88010 ${\beta}$-glucosidase activity were pH 5.0 and ${37^{\circ}C}$, and addition of divalent cations to the reaction mixture resulted in a notable decrease in enzyme activity. The ${\beta}$-glucosidase activity was enhanced twofold when W. cibaria KFRI88010 was grown in a medium containing fructose as compared with to a medium containing glucose or cellobiose.

• Journal of Life Science
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• v.8 no.4
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• pp.387-394
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• 1998

A thermophilic bacterium (strain DG0303) producing a thermostable $\alpha$-glucosidase was isolated from manure and identified as Bacillus sp. Strain DG0303 produced high level of $\alpha$-glucosidase compared with other thermophilic Bacillus strains. The cellular protein patterns were also compared with other Bacillus strains by sodium dodecyl sulfatepolyacrylamide gel electrophoresis(SDS-PAGE). On the basis of 16S rDNA analysis the Bacillus sp. DG0303 was found to be a member of Bacillus rDNA group 5. The optimum temperature for growth was 65$\circ$C and no growth was obtained at 40$\circ$C or 75$\circ$C. The optimum pH for growth was 5.5 to 8.5. $\alpha$-glucosidase activity was produced during growth and most activity was detected in the culture supernatant. The $\alpha$-glucosidase production was constitutive in the absence of carbohydrates. High level of enzyme activity was detected when the culture was grown on medium containing starch. Addition of glucose resulted in the repression of the $\alpha$-glucosidase production. The optimum pH and tempoerature for enzyme activity were pH 5.0 and 65$\circ$C, respectively. When analyzed by zymogram, the culture supernatant showed a single $\alpha$-glucosidase band with a molecular weight of approximately 60,000.

• Mycobiology
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• v.43 no.1
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• pp.57-62
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• 2015

${\beta}$-Glucosidase, which hydrolyzes cellobiose into two glucoses, plays an important role in the process of saccharification of the lignocellulosic biomass. In this study, we optimized the activity of ${\beta}$-glucosidase of brown-rot fungus Fomitopsis pinicola KCTC 6208 using the response surface methodology (RSM) with various concentrations of glucose, yeast extract and ascorbic acid, which are the most significant nutrients for activity of ${\beta}$-glucosidase. The highest activity of ${\beta}$-glucosidase was achieved 3.02% of glucose, 4.35% of yeast extract, and 7.41% ascorbic acid where ascorbic acid was most effective. The maximum activity of ${\beta}$-glucosidase predicted by the RSM was 15.34 U/mg, which was similar to the experimental value 14.90 U/mg at the 16th day of incubation. This optimized activity of ${\beta}$-glucosidase was 23.6 times higher than the preliminary activity value, 0.63 U/mg, and was also much higher than previous values reported in other fungi strains. Therefore, a simplified medium supplemented with a cheap vitamin source, such as ascorbic acid, could be a cost effective mean of increasing ${\beta}$-glucosidase activity.

• International Journal of Industrial Entomology and Biomaterials
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• v.34 no.2
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• pp.38-44
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• 2017

Mulberry leaves containing 1-deoxynojirimycin (DNJ) have been recognized as a potentially important source for prevent or treat hyperglycemia. However, DNJ content of natural mulberry leaf are as low as 0.1%. Thus, the most effective method for increasing ${\alpha}$-glucosidase inhibitory activity with the DNJ high-production is needed. In this study, we investigated the influence of ${\alpha}$-glucosidase inhibitory activity according to different pH values (6-9) and inoculation amounts (0.1-0.5%) when Bacillus subtilis cultured on mulberry leaf powder media. We confirmed that ${\alpha}$-glucosidase inhibitory activity was difference according to culture conditions of different pH values, inoculation amounts, and fermentation times. The results of mulberry leaf fermentation according to pH values and inoculation amounts were shown that the optimal conditions for ${\alpha}$-glucosidase inhibitory activity were defined as pH 7 and 9, inoculation amount 0.4%, and incubation until 2 to 4 days. These results can be provided a basic data for the optimal culture conditions increasing ${\alpha}$-glucosidase inhibitory activity from mulberry leaf fermentation.

• Biomedical Science Letters
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• v.13 no.3
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• pp.245-249
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• 2007

We investigated the fibrinolytic and ${\alpha}-glucosidase$ inhibitory activity of 55 wild mushroom methanol extracts. Among them, 14 mushrooms showed fibrinolytic activity. In particular, Amanita virgineoides showed the greatest enzyme activity (3.9 plasmin units/ml) by a fibrin plate assay. The fibrinolytic activities of Suillus pictus and Polypolellus varius were 3.8 plasmin units, and the activity of Gomphus fujisanensis was 2.8 plasmin units. Leccinum extremiorientale and Xerocomus nigromaculatus had the same activity with 2.3 plasmin units. In a ${\alpha}-glucosidase$ inhibitory activity test, Lactarius sp. showed the greatest inhibitory activity at 97.3%. The ${\alpha}-glucosidase$ inhibitory activities of Clitocybe odora, Xerocomus nigromaculatus, Melanoleuca melaleuca, Suillus pictus, and Gyroporus castaneus were 84.3%, 77.9%, 74.6%, 68.7%, and 65.4%, respectively. According to the results, because Suillus pictus and Xerocomus nigromaculatus have strong fibrinolytic and ${\alpha}-glucosidase$ inhibitory activities, the two mushrooms will be used as materials for the development of new biofunctional food.

• The Korean Journal of Food And Nutrition
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• v.34 no.3
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• pp.289-294
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• 2021

The antioxidant activity and α-glucosidase inhibitory activity of the solvent fraction fractionated from the methanol extract of Saururus chinensis Baill were examined. As a result of measuring the yields of methanol, hexane, chloroform, ethylacetate, butanol, and water fractions, the extraction yield of fraction was 18.60, 3.38, 24.03, 7.75, 8.11 and 62.57%, respectively. The total polyphenol content of the methanol extract of Saururus chinensis Baill was 13.40, 4.62, 7.39, 31.24, 25.76 and 5.64 mg GAE/g, respectively. DPPH radical scavenging activity (IC_50%) results were 20.81, 5.47, 10.15, 22.63, 19.68 and 21.06 ug/mL, respectively, and hydroxyl radical scavenging activity (IC_50%) results were 15.81, 2.69, 8.84, 12.80, 3.70 and 3.39 ug/mL. Hydrogen peroxide scavenging activity scavenging activity measurement (IC_50%) showed 33.63, 8.88, 16.93, 32.84, 33.79, and 33.71 ug/mL in methanol, hexane, chloroform, ethyl acetate butanol, and water fractions, respectively. The α-glucosidase inhibitory activity of the solvent fraction fractionated with the methanol extract of 300 sec was measured for the α-glucosidase inhibitory activity of methanol, hexane, chloroform, ethyl acetate butanol, and water fraction, respectively, 15.85, 10.84, 15.74, 24.90, 2.58 and 35.70%.

• KSBB Journal
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• v.15 no.1
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• pp.9-13
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• 2000

In order to determine the characteristics of $\beta$-glucosidase associated with cellulose degradation, the enzyme produced extracellularly by the mycelia of Tricholoma matsutake DGUM 26001 in culture broth was partially purified. The enzyme activity was maintained in the range of temperatures trom 55 to $70^{\circ}C$ and its optimum temperature was $65^{\circ}C$. The $\beta$-glucosidase enzyme showed relatively high activity in the range of pH 3.0-5.0 and its optimum pH was 4.0. Under the optimal conditions, the specific activity of $\beta$-glucosidase for salicin as a substrate was 18.7 unit/mg protein. After thermal treatment of the enzyme at $55^{\circ}C$ for 60 min, more than 90% of the enzyme activity was still sustained. Iron($Fe^{++}$) stimulated enzyme activity, whereas mercury($Hg^{++}$) and copper($Cu^{++}$) inhibited. Compared to salicin as a substrate, the relative activity for cellobiose was observed to be 48.6%. The apparent $K_m$ and $V_{max}$ of the enzyme with cellobiose were 0.12 mM and 0.02 umol/min, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.44 no.7
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• pp.993-999
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• 2015

For the purpose of investigating the in vitro antidiabetic activity of a medicinal herb and herb mixture extracts prepared through traditional antidiabetic prescription, this study examined ${\alpha}$-glucosidase inhibitory activity. Tyrosinase, a type I membrane glycoprotein, is synthesized and glycosylated in the endoplasmic reticulum (ER) and Golgi. The enzyme is subsequently transported to melanosomes, where it participates in melanogenesis. Previous studies showed that disruption of early ER N-glycan processing by an ${\alpha}$-glucosidase inhibitor suppresses tyrosinase enzymatic activity and melanogenesis. According to the results, most oriental medicinal herbal extracts were stronger than acarbose and N-butyldeoxynojirimycin, known as an ${\alpha}$-glucosidase inhibitor. Interestingly, ethyl acetate layer of enzyme hydrolyzed Cheongsimyeonjaeum had an inhibitory effect on melanin synthesis in B16F1 cells, although it did not inhibit tyrosinase activity directly. Together, ${\alpha}$-glucosidase inhibition activity could be used to evaluate anti-melanogenesis, although cross-checking with melanin inhibitory assay is recommended.