• YAKHAK HOEJI
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• v.32 no.5
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• pp.304-307
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• 1988

394 strains of soil microorganism were isolated from the Korean soil samples. The isolated strains were shake-cultured in oat-meal medium. The filtrates of the cultures were screened for the production of ${\alpha}-amylase$ inhibitors. Five strains were identified to produce ${\alpha}-amylase$ inhibitors. And these strains were identified as Actinomycetes.

• Journal of Korean Biological Nursing Science
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• v.25 no.4
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• pp.306-315
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• 2023

Purpose: This study aimed to evaluate the rest-activity circadian rhythm (RAR) using data obtained from wearable actigraph devices in hospitalized older adults with mild cognitive impairment (MCI), and to investigate its relationship with salivary alpha amylase (sAA). Methods: This secondary data analysis used data from the Hospitalized Older Adults' Cognition and Physical Activity Study. Actigraph data for 3-4 days were analyzed for RAR. RAR indices such as interdaily stability (IS), intradaily variability (IV), activity level during the most active 10-hour period and during the most least active 5-hour period, and relative amplitude (RA) were calculated. Data on sAA collected in the morning and general characteristics, including body mass index (BMI), were analyzed. Results: Data from 92 hospitalized older adults with MCI were analyzed. The IS, IV, RA were 0.23, 0.73, 0.88, respectively. The average level of sAA was 77.02 U/mL, and a higher level of sAA was significantly associated with better IS and RA in the regression analysis, while age, BMI, and cognitive level were not. BMI showed positive correlations with IS and RA. Conclusion: RAR in the hospitalized older adults with MCI was attenuated, showing especially low IS, which implies they failed to maintain regular and repetitive 24-hour RAR. Increased sAA and BMI were associated with robust RAR. Nurses need to pay attention to maintain robust RAR in hospitalized older adults with MCI, and strategies should be developed to improve their RAR.

• The Korean Journal of Mycology
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• v.6 no.2
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• pp.1-10
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• 1978

In de novo biosynthesis of the extracellulor enzymes-proteinsaes, alpha and gluc-amylases during the synchronized differentiation of Aspergillus niger in submerged culture and surface liquid culture were investigated. Gluc-amylase was synthesized in the stage of presporulation in which phialide formation is involved. Proteinase was synthesized both in the stages of conidiophore formation and presporulation. Alpha-amylase was synthesized during presporulation and sporulation stages, the activity of enzyme lasted for seven days on surface liquid culture. It seemed that the synthesis was occured in de novo partly repressed by the catabolite, and its nature was found to be constitutive since it is produced in non-starch medium. Polyacrylamide gel electrophoresis have shown that presporulating and sporulating body produced diverse types of the proteins whereas the earlier stages of vegetative body showed simpler profiles. The uptake of C-14 uracil into RNA and C-14 glutamate into protein were shown to be vigorous in presporulating body rather than those in sporulating body. Coincidence of alpha-amylase biosynthesis in de novo and sporulation may be significant in the study of differentiation in which gene expression is involved.

• Korean Journal of Microbiology
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• v.46 no.1
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• pp.80-85
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• 2010

Two different ${\alpha}$-amylase isozymes (AMY1 and AMY2) found in barley malt share up to 80% of amino acid sequence identity with each other, but their enzymatic properties differ remarkably. AMY1 shows the highest activity at low concentration of calcium ion, while AMY2 is highly active at high calcium concentration. Meanwhile, BASI (Barley ${\alpha}$-Amylase/Subtilisin Inhibitor) protein specifically inhibits only AMY2. In the present study, three separate regions in AMY genes (I, II, and III) were assigned on the basis of restriction enzyme sites and four kinds of chimeric amylases have been obtained by swapping a part of regions with each other. Each chimera gene was successfully over-expressed in Pichia pastoris. From the results of enzymatic characterization, both AMY211 and AMY122 showed the mixed or intermediate type of calcium-dependent activity between AMY1 and 2. Meanwhile, only AMY221 chimera could be significantly inhibited by BASI protein. As a result, it can be proposed that some amino acid residues in the region I and II, except region III, of barley ${\alpha}$-amylases play very important roles in calcium-dependency and interaction with BASI.

• Microbiology and Biotechnology Letters
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• v.38 no.2
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• pp.151-157
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• 2010

Barley malt produces two different $\alpha$-amylase isozymes (AMY1 and AMY2), which share up to 80% of amino acid sequence identity with each other. However, their enzymatic properties differ remarkably. In this study, five chimeric enzymes between AMY1 and 2 were constructed by staggered extension process (StEP) technique, and their enzymatic properties were characterized. According to the results, chimeric AMY-D2, D8, and E12 showed the mixed or intermediate types of calcium-dependent activity between AMY1 and 2. Meanwhile, only AMY-E10 chimera could be significantly inhibited by barley $\alpha$-amylase/subtilisin inhibitor (BASI) protein. Chimera AMY-C6 showed the same calcium-dependency as AMY1, while AMY-E10 was closely similar to AMY2. As a result, it can be proposed that some amino acid residues in the region II, III, and IV of barley $\alpha$-amylases can play very important roles in the interaction with BASI, and those in III, V, VI, and VII may partly affect on the calcium-dependent activity.

• Journal of Food Hygiene and Safety
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• v.13 no.1
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• pp.20-23
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• 1998

The objective of this study was to evaluate the bifidogenic effect and a-glucosidase inhibitory effect of artificially cultured Phellinus linteus. The water extract of P. linteus promoted the growth of Bifidobacterium breve as well as the decrease of final pH in the media culturing intestinal bacteria. The growth of lactic acid bacteria inhibited effectively the bacterial enzymes, ${\beta}-glucosidase,\;{\beta}-glucuronidase$ and tryptophanase, of intestinal bactetria. The water extract of P. linteus inhibited maltase, sucrase and ${\alpha}-amylase$ of rat intestine.

• Biomolecules & Therapeutics
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• v.1 no.1
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• pp.26-30
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• 1993

Strain of treptomyces minoensis DMCJ-144 was tried to be improved so that it produces much more the $\alpha$-amylase inhibitor. Streptomyces minoensis DMCJ-144 was treated with 1 mg/mι (pH 9.0) of N-methyl-N'-nitro-N-nitrosoguanidine at $30^{\circ}C$ for 60 min and irradiated with UV light distanced 30 cm for 20 min. After mutagenesis, surviving colonies were cultured on the CM contaning acriflavine ($10{\mu}g/ml$) three times in order to enhance the mutability. And then through multi-level screening, colonies that ${\alpha}$-amylase inhibitor productibility. was Improved were selected by modified-blue value method. After third acriflavine treatment, $\alpha$-amylase inhibitory activities of selected colonies were found to be much better as compared with that of parent strain. One mutant strain showed 5.4 time inhibitory activity than the parent strain.

• YAKHAK HOEJI
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• v.33 no.3
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• pp.175-182
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• 1989

To find ${\alpha}-amylase$ inhibitors produced by microorganisms from soil, a strain which had a strong inhibitory activity against bacterial ${\alpha}-amylase$ was isolated from the soil sample collected in Korea. The morphological and physiological characteristics of this strain on several media and its utilization of carbon sources showed that it was one of Streptomyces species according to the International Streptomyces Project method. The amylase inhibitor of this strain was purified by active carbon adsorption, silicagel column chromatography, SP-Sephadex C-25 column chromatography, adsorption on Amberlite XAD-2. The inhibitor was oligosaccharide which was composed of glucose. The inhibitor had inhibitory activity against other amylase such as salivary ${\alpha}-amylase$, pancreatic ${\alpha}-amylase$, fungal ${\alpha}-amylase$ and gluco-amylase.

• Korean Journal of Microbiology
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• v.26 no.2
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• pp.73-81
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• 1988

$\alpha$-Amylase (EC.3.2.1.1) of Neurospora crassa (ATCC9279) was cloned in E. coli HB101 using shotgun method, and the enzymes isolated from both N. crassa and E. coli were compared. Chromosomal DNA isolated from the spores of N. crassa was partially digested with PstI restriction endonuclease and rejoined to pBR322 which had been digested with the same enzyme. The resulting recombinant DNA were introduced into E. coli HB101 which had competancy by treating with $CaCl_{2}$. As the result, about 8000 colonies which showed tetracycline resistance were selected and two of the colonies which had 13.5Kb recombinant plasmid exhibit starch degrading activity on starch-containing plate when treated with D-cycloserine. $\alpha$-Amylases from both N.crassa and E. coli were isolated by using ammonium sulfate precipitation, DEAE-cellulose ion exchange column chromatography and Bio-Gel P150 gel foltration column. As the result, about 81.3 fold and 5.6 fold purifications in specific activities were obtained respectively, and specific activities of the gel filtrates were 6.1u/mg and 85u/mg respectively. The properties of both enzymes were compared and they showed quite the similar patterns in optimal temperature, optimal pH and had same molecular weight about 100,000 daltons on gel filtration method. Optimal temperatures for both enzymes were $70^{\circ}C$ and optimal pH were about 6 and 10.

• Microbiology and Biotechnology Letters
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• v.16 no.5
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• pp.358-362
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• 1988

Aqueous two-phase fermentation system was tested for the overproduction of extracellular enzyme through $\alpha$-amylase fermentation by Bacillus amyloliquefaciens. By employing aqueous two-phase system $\alpha$-amylase activity showed 25% increase compared to the result using regular medium and no deactivation of the enzyme was observed. The presence of polyethylene glycol was observed to promote the enzyme production, while to inhibit the growth of the microorganism. It is recommended that polyethylene glycol be added during the log-growth phase and dextran be added after the enzyme activity reaches Its maximum for efficient $\alpha$-amylase fermentation and in situ recovery of the enzyme.