• Applied Biological Chemistry
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• v.40 no.6
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• pp.484-489
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• 1997

The characteristics of growth and esterase activity of bacterial strains isolated from acid hydrolysed soybean protein were examined. All the isolated strains having decomposition activity of p-hydroxybenzoic acid butyl ester and esterase producing activity were identified as Bacillus sp. by morphological and biochemical methods. The specific growth rates, esterase activities and p-hydroxybenzoic acid butyl ester decomposition activities of isolated strains were $0.844{\sim}1.213\;h^{-1}$, $21{\sim}222\;mU/ml$ and $5.4{\sim}8.1\;mU/ml$, respectively. In the fermentation of Bacillus sp. KB8 strain which had the highest esterase producing activity, growth, extracellular excretion and intracellular synthesis of esterase were inhibited by adding NaCl in the culture broth. Esterase producing activity gradually increased after late exponential growth phase, until maximum value of 420 mU/ml reached after 64 hours culture period. Esterase of Bacillus sp. KB8 strain was stable up to $50^{\circ}C$ for 30 minutes, but was inactivated by heating for 30 minutes at $70^{\circ}C$. The enzyme activity exponentially decreased during the incubation time at the temperatures of $60^{\circ}C$ and $65^{\circ}C$.

• Korean Journal of Environmental Agriculture
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• v.9 no.2
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• pp.97-103
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• 1990

In order to determine the major biochemical degradation factors of the two organophosphorus insecticides, diazinon and dursban, the activities of monooxygenase(m. o.) and ${\alpha}$, ${\beta}-esterase$ were studied in submerged soil under laboratory conditions at $30{\pm}1^{\circ}C$ The degradation rate of diazinon by microorganism showed 1.5 times higher than dursban. The m. o. activity increased from 12hrs and 3days after application of diazinon and dursban, respectively. But the ${\beta}-esterase$ activity showed maximum at one day after application of dursban and $5{\sim}8$ days after diazinon application. Also, the ${\beta}-esterase$ activity was about 10 times higher than ${\alpha}-esterase$. Hence, it was concluded that the biological degradation of diazinon was mainly attributed to m. o. activity and the degradation of dursban to ${\beta}-esterase$ activity.

• Journal of The Korean Society of Grassland and Forage Science
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• v.12 no.4
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• pp.253-259
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• 1992

The esterase isozyme in tissue of wild legume plants were separated by horizontal starch gel electrophoresis. Extracts used in this study were prepared from fully expanded young leaf, cotyledon and radicle of seedling and root-nodule of Glycine sola, Vigna vexillata var. tsuscmensis and Trifoliwn repens. The results are as follows; 1. Each tissue examined had a characteristic banding pattcrn. Number of bands in each species, G. soja, V. vexillata, and T . repens, were 14, 8 and 1 1 bands, respectively. And difference in esterase isozyme bands were greater from tissue to tissue than difference between habitat. 2. Est-I, Est-2. Est-3 and Est-4 in G. soja, Est-I in V. vexillata and Est-l and Est-2 in T. repens showed strong cnzyme activity than other enzyme. 3. Esterase isozyme variation in G. soja and T . repens showed more variety than V. vexillata. This is resulted from many genotypic differences within species. 4. The main enLyme among thc esterase isozyme were Est-I. Est-2, Est-3 and Est-4.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.53-56
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• 2000

A thermostable esterase from the hyper thermophilic archaeon Sulfolobus solfataricus was partially purified 590-fold with $16.2\%$ recovery. The partially purified esterase had a specific activity of $29.5\;{\mu}mol\;min^{-1}mg^{-1}$ when the enzyme activity was determined using p-nitrophenyl butyrate as a substrate. The apparent molecular weight was about 100 kDa, while the optimum temperature and pH for esterase were $75^{\circ}C$ and 8.0, respectively. The enzyme showed high thermal stability and solvent tolerance in comparison to its mesophilic counterpart. The enzyme also showed chiral resolution activity for (S)-ibuprofen, indicating that S. solfataricus esterase can be used for the production of commercially important chiral drugs.

• Microbiology and Biotechnology Letters
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• v.22 no.6
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• pp.599-606
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• 1994

Bacillus stearothermomophilus, a strong xylan degrader, was confirmed to express multiple esterase activities in addition to the major xylanolytic enzymes. One of the genes encoding the esterases was isolated from the genomic library of B. stearothermophilus constructed with EcoRl restriction endonuclease and pBR322 plasmid. Three recombinant plasmids showing the tributyrin degrading activity were selected from approximately 7, 000 E. coli HB101 transformants, and were found to have the same insert of a 3.2 kb DNA fragment. Restriction mapping and hybridization studies revealed that the gene(estII) on the hybrid plasmid (pKMG7) had originated from the B. stearothermophilus chromosome, and was distinct from the estl, another esterase gene of B. stearothermophilus isolated in the previous work. The E. coli cells harboring pKMG7 produced an acetylxylan esterase that exibited similar substrate specificity to the esterase encoded by the estI gene.

• Journal of Microbiology and Biotechnology
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• v.18 no.5
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• pp.889-896
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• 2008

A suitable simple model tested by experiments is required to address complex biological reactions like esterase synthesis by Saccharomyces cerevisiae. Such an approach might be the answer to a proper bioprocessing strategy. In this regard, a logistic model for esterase production from Saccharomyces cerevisiae has been developed, which predicts well the cell mass, the carbon source (glucose) consumption, and the esterase activity. The accuracy of the model has been statistically examined by using the Student's t-test. The parameter sensitivity analysis showed that all five parameters (${\mu}_m$, $K_a$, $X_m$, $Y_{x/s}$, and $Y_{p/x}$) have significant influence on the predicted values of esterase activity.

• Journal of The Korean Society of Grassland and Forage Science
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• v.14 no.2
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• pp.82-87
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• 1994

This study was planned to identify the variety of Italian ryegrass using electrophoresis. Thirty seven varieties of Italian ryegrass were tested by starch gel electrophoresis. The specific electrophoretic zymograms of each variety were observed by Alcohol dehydrogenase(ADH) and Esterase. The results were surnrnerized as follows; 1. AU varieties displayed two band zones by ADH and Rf values were 0.63 and 0.6 (Table 2, Fig. 2). 2. There were five band type for ADH isozyme of 37 varieties classified with isozyme banding pattern. According to the isozyme band type 7, 2, 6, 18 and 4 varieties belong to group, I, II, III, IV, and V, respectively (Table 2). 3. The varieties displayed single band zone for Esterase isozyme and Rf value was 1.00 (Table 2, Fig. 4). 4. According to banding type, Esterase isozyme of 37 varieties classified into 3 groups, 22, 8 and 7 varieties belong to group, I , II, and III, respectively (Table 2).

• KOREAN JOURNAL OF CROP SCIENCE
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• v.41 no.3
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• pp.332-339
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• 1996

Electrophoretic method was utilized to classify 100 varieties of sweet potato germplasm maintained at the National Crop Experiment Station of Korea in 1993. The esterase isozyme patterns in the leaves were classified into 14 different types. Type Ⅸ included the most of the varieties (46) tested and Ⅶ, I, III, Ⅷ, II and V types of all included 47 varieties in order. The other 7 varieties had different band pattern with each other. Type I having many kind of band pattern included Shinyulmi, Beniastma and High starch which had the dry type of tuberous roots varieties. The esterase isozymes pattern in the tuberous roots were classified with 18 kinds of types. The C type included 22 varieties and B, K, A, E, I and N in order. The proteins pattern in the tuberous roots were classified with 7 kinds of types. I type included 36 varieties, and IV type included 27 varieties and II, III, Ⅶ and Ⅵ types in order.

• Journal of Microbiology and Biotechnology
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• v.6 no.3
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• pp.173-178
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• 1996

Synergic effects among endo-xylanase, $\beta$-xylosidase, and acetyl xylan esterase of Bacillus stearothermophilus in the hydrolysis of xylan were studied by using birchwood, oat spelt, and acetylated xylan as substrates. Synergism between endo-xylanase and $\beta$-xylosidase was observed on all three substrates tested, indicating that $\beta$-xylosidase enhanced the production of xylose by relieving the end-product inhibition upon endo-xylanase conferred by xylooligomers. Endo-xylanase and $\beta$-xylosidase also showed synergism with acetyl xylan esterase in the hydrolysis of birchwood and acetylated xylan, while no synergic effect was detected in oat spelt xylan hydrolysis. Thus, the hydrolysis of xylan containing acetic acid side chains required the action of acetyl xylan esterase, which eliminated the steric hindrance of the side chains, leading to the better hydrolysis by endo-xylanase and $\beta$-xylosidase , and the acetyl xylan esterase activity was also enhanced by endo-xylanase and $\beta$-xylosidase for the latter enzymes provided acetyl xylan esterase with shorter xylan oligomers, the better substrate for the enzyme.

• 한국생물공학회:학술대회논문집
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• 2001.11a
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• pp.625-628
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• 2001

To isolate novel strains that hydrolyzed the rac-ketoprofen ethyl ester to ketoprofen in the stereospecific manner, we screened broad ecological niches and soil samples in which the activity was expected to be found. From thousands of strains, we isolated a Pseudomonas sp. S34 producing a (S)-stereospecific esterase, and a thermostable esterase with (R)-form selectivity was also 。 btained from Bacillus stearothermophilus JYl44. To further analyse the gene structure and to induce a high level expression, two genes from each strain were cloned and sequenced. BLAST search results with the esterase gene from 534 revealed that both of gene (80-84 %) and amino acid sequences (89- 95 %) were highly conserved in the related esterases from Pseudomonas strains (fluorescens and aeruginosa). The thermostable esterase from JY144, however, revealed a relative low homology (45-52 %) to other esterase and/or lipase from related strains. Obviously, a complete conversion with pure enantiomer (R - or S) were readily achieved by recombinant clones expressing either (R)- or (S)- stereospecific esterase.