• Microbiology and Biotechnology Letters
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• v.19 no.5
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• pp.477-486
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• 1991

To elucidate enzymatic properties of a-glactosidase (EC 3.2.1.22) from Asp. niger, a-galactosidase from wheat bran culture was purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. And then its enzymatic propeties were investigated. The highest level of $\alpha$-galactosidase activity was obtained when Asp. niger was grown on wheat bran medium at $30^{\circ}C$ for 96 hours. The $\alpha$-galactosidase was purified by 23.7 fold by ammonium sulfate fractionation, ion exchange chromatography on DEAE-Celluose and Sephadex A-50, and gel filtration on Sephadex G-150 and its specific activity was 1,229 Unitslmg protein and the yield was 14% of the total activity of wheat bran culture. The purified $\alpha$-galactosidase was found to be homogeneous by polyacrylamide gel electrophoresis and HPLC. The $\alpha$-galactosidase was a tetrameric glycoprotein which consisted of identical subunits with molelcular weight of 28,000 each by SDS-PAGE and isoelectric point was determined analytical isoelectric focusing to be pH 4.6. The optimal temperature and pH for the $\alpha$-galactosidase activity were $40^{\circ}C$ and pH 6.5, respectively, and 54% of its activity was lost by heating at $60^{\circ}C$ for 10 mins, It was appeared to have higher affinty to raffinose than to stachyose. The K, value and activation energy of $\alpha$-galactosidase were 5.0 mM and 8.515 Kcal per mole for p-nitrophenyl- $\alpha$--D-galactopyranoside, respectively.

• YAKHAK HOEJI
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• v.53 no.3
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• pp.114-118
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• 2009

Bioemulsifiers are those chemicals which are produced from microorganisms but which have both hydrophilic and hydrophobic groups. $\alpha$-Glucosidase inhibitor ($\alpha$-GI) produced from Bacillus lentimorbus B-6 (B-6) showed bioemulsifying activity. But $\beta$-glucosidase inhibitor produced from B-6 didn't show emulsifying activity. $\alpha$-GI was purified from supernatant of B-6 grown in minimal culture medium containing glucose and sodium glutamate by Sephadex G-100 column chromatography and isolated from $\beta$-GI by dialysis against water. Toluene was determined as the best substrate for emulsifying activity of $\alpha$-GI. $\alpha$-GI showed thermostability at $100^{\circ}C$ for 15 min, high salt tolerance up to 32% NaCl and wide range of pH-stability at pH $4\sim10$. Emulsifying character of $\alpha$-GI can be useful for the liposome formation for the treatment of diabetes mellitus.

• Bulletin of the Korean Chemical Society
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• v.27 no.7
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• pp.1001-1004
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• 2006

The m-calpain activity hydrolyzing a fluorogenic substrate of N-Succinyl-Leu-Leu-Val-Tyr-7-amino-4-methylcourmarin (LLVY-AMC) was significantly stimulated by more than two-fold in the presence of 5$\mu$M $\alpha$synuclein at $15{^{\circ}C}$. The stimulation was also confirmed with azocasein. The stimulation of the peptide hydrolyzing activity required structural intactness of $\alpha$-synuclein since the C-terminally or N-terminally modified proteins such as $\beta$-synuclein, $\alpha$-syn1-97, and $\alpha$-syn61-140 did not increase the proteolytic activity. Instead, however, the N-terminally truncated $\alpha$-syn61-140 was shown to drastically suppress the calpain activity. Since the N-terminal truncation was known to be the primary cleaving event of calpain-mediated proteolysis of $\alpha$-synuclein and the $\alpha$-syn61-140 has been demonstrated to be resistant against the calpain digestion, it has been proposed that the intracellular calpain activity could be regulated in a reciprocal manner by $\alpha$-synuclein and its proteolyzed C-terminal fragment. Based on the results, a possible physiological function of $\alpha$-synuclein has been suggested as a calpain regulator which contains both stimulatory and inhibitory activities.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.25 no.3
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• pp.87-99
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• 1999

Manuka oil named New Zealand’s tea tree oil is oil-soluble and comes firom nature. Manuka oil and its extract $\alpha$-pinene, Oxy’less clear, R-limonene which is one of the component of Citron extracted from Grapefruit seed and Citrex were used to estimate the antimicrobial activity and to improve the capability of antiseptic. Disk diffusion method was used to measure the antimicrobial activity. Escherichia coli which is gram-negative bacteria and Staphylococcus aureus which is gram-positive bacteria were used as strain. The antimicrobial activity of Manuka oil and $\alpha$-pinene for Escherichia coli, Staphylococcus aureus was similar when the concentration of Manuka oil and $\alpha$-pinene are 10u/paper disk. However, antimi-crobial activity of Manuka oil fDr Escherichia coli, Staphylococcus aurem was better than that of $\alpha$-pinene when the concentration of Manuka oil and $\alpha$-pinene was low. Antimicrobial activity of Oxy’less clear is better than that of propyl para hydroxybenzoate(PPHB), R-limonene at all the concentration and is similar to that of $\alpha$-pinene. Antimicrobial activity.

• Journal of Pharmaceutical Investigation
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• v.21 no.3
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• pp.143-147
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• 1991

${\alpha}-amylase$ was immobilized on the surface of polyethylene glycol(M.W. 2000) grafted polyurethane film using diisocyanate in an attemp to develop enzyme immobilized polymeric materials. The surface morphology of the modified polyurethane film was examined by SEM. Effects of pH and temperature on the activity of the immobilized ${\alpha}-amylase$ were investigated. The optimal pH range of the activity was $7.0{\sim}7.5.$ The immobilized ${\alpha}-amylase$ demonstrated high thermal stability and maintained consistent activity during long-term storage.

• Korean Journal of Plant Resources
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• v.22 no.1
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• pp.71-77
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• 2009

Antioxidative activity and ${\alpha}$-amylase inhibitory activity were investigated in the methanol extracts of 289 species of angiosperm plants native to Jeju Island in order to select the plant species containing bioactive materials for functional foods or medicines. The antioxidative activity, estimated by the DPPH radical scavenging capacity, was high in the galla of Rhus chinensis, the fruit of Platycarya strobilacea, and the stem of Cedrela sinensis. Particularly, the antioxidative activity of Rhus chinensis galla (94.2${\pm}$0.8%) was very high even though compared to those of BHA (61.7${\pm}$0.6%) and ascorbic acid (53.6${\pm}$0.7%). The ${\alpha}$-amylase inhibitory activity was 80% or above in 9 species including Cornus macrophylla (stem, leaf), Distylium racemosum (leaf) and Vaccinium oldhami (leaf). These results suggest that these plants could be potentially utilizable to develop bioactive materials for functional foods or medicines.

• Journal of Radiation Protection and Research
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• v.11 no.2
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• pp.130-138
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• 1986

A study on the measurement of alpha activity in ground air has been carried out using CA 80-15 and LR 115-1 cellulose nitrate nuclear track detectors. The detection efficiency of the detectors were determined by making use of an $^{241}Am$ alpha source of $0.1{\mu}Ci$ in activity under a known geometrical arrangement. For the field measurement of alpha activity of emanated radon and its progeny in ground air two different radon cups were installed for a certain period of time in two neighbouring ground holes of about 15 cm in diameter and 45 cm in depth. Of the two radon cups one kept closed space during the detecting period, while the other kept open space with a hole enabling the air to ventilate. The etched tracks were read out by a microscope and the results obtained through statistical analysis were evaluated in terms of alpha activity per unit volume of air.

• Mycobiology
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• v.39 no.4
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• pp.278-282
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• 2011

The objective of this study was to find useful fungi with ${\alpha}$-amylase activity from the Korean traditional nuruk for the quality of traditional Korean alcoholic beverage. In this study, 165 samples of traditional nuruk were collected from 170 regions throughout Korea and the fungi were isolated to a total of 384 strains. In order to investigate the effect of microflora on nuruk, ${\alpha}$-amylase activity, saccharogenic power (SP), starch hydrolysis activity and acid producing activity were evaluated. Ten strains were selected by ${\alpha}$-amylase activity, which ranged from 458.47 to 1,202.75 U/g. The size of the discolored zone for the starch hydrolysis activity of each fungus ranged from 0.3 to 2 cm. The SP of the 10 strains ranged from 228.8 to 433.4 SP. Of the 10 stains, three were identified as Aspergillus oryzae, two as Aspergillus flavus, two as Lichtheimia sp., one as Rhizopus oryzae and two as other strains. The total aflatoxins present in the nuruks were examined using enzyme-linked immunosorbent assay. The 10 nuruks had less than 1.11 ppb of aflatoxins.

• 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.

• Journal of Applied Biological Chemistry
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• v.43 no.3
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• pp.141-146
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• 2000

Glycosidase activities were tested from the grape berries, Vitis labruscana B. Takasumi. Among various glycosidases, $\alpha$-D-galactosidase was found to be the most active in the flesh and other glycosidases were considerably active in the order of the following: $\alpha$-D-mannosidase>$\alpha$-D-glucosidase>$\beta$-D-glucosidase>$\beta$-D-galactosidase. In the seeds, $\alpha$-D-glucosidase activity was the highest and other glycosidases such as $\alpha$-D-galactosidase, $\beta$-D-glucosidase, and $\beta$-D-galactosidase were still significantly active. The $\alpha$-D-galactosidase in the grape flesh was purified over 83-folds through salting-out with $(NH_4)_2SO_4$ and a series of chromatographies employing Sephadex G-50, Octyl-Sepharose, Q-Sepha- rose, and Biogel P-100. The enzyme was a monomer of 45 kDs as determined through SDS-PAGE and Sephacryl S-200 chromatography. The purified enzyme showed a preference of $\alpha$-D-galactose to $\beta$-D-galactose as a substrate about 5.4 times. Sulfhydryl specific reagents such as N-ethylmaleimide and iodoacetamide significantly inhibited the enzyme activity to the extents of 48 and 52% of its initial activity, respectively. The optimumpH range of $\alpha$-D-galactosidase was around 6.5-7.0. The enzyme activity increased by 46% in the presence of 1mM $Fe^{2+}$.