• Microbiology and Biotechnology Letters
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• v.47 no.1
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• pp.87-95
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• 2019

Esterase produced by Acinetobacter sp. B1 (strain B1) was optimized by means of one-variable-at-a-time and response surface methodologies. Results of the one-variable-at-a-time experiment showed that Tween 80 significantly increased esterase production of strain B1. The addition of Tween 80 to the culture medium increased the biomass and esterase activity of strain B1, stimulated content of total extracellular protein, and enhanced the oleic acid (C18:1) composition in the cell membrane of strain B1. The influence of eight culture variables on esterase production was evaluated by Plackett-Burman design. Results showed that Tween 80, pH, and $K_2HPO_4$ significantly affected the esterase production of strain B1. Tween 80, pH, and $K_2HPO_4$ were further optimized by central composite design. Under the optimized conditions (w/v, soluble starch 2.5%, tryptone 1.5%, Tween 80 0.8%, $K_2HPO_4$ 0.5%, NaCl 0.5%, pH 8.0, inoculum size 1%, and inoculum age 24 h), the maximum esterase activity of strain B1 was 152.13 U/ml, which was 10-fold higher than that of non-optimization after 36 h cultivation.

• International Journal of Industrial Entomology and Biomaterials
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• v.9 no.1
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• pp.59-63
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• 2004

By using PAGE, a study was made on the nonspecific esterase spectra of female genital organs and eggs in Bombyx mori L. The expression of 11 esterase bands was detected during ontogenesis of races and inter-races hybrids kept in Bulgaria. The gene activity of 9 esterase loci was assumed. Esterases specific for the spectrum of diapausing eggs were observed. In two esterase zones, intra- and inter-breed polymorphism was found. Based on the same breed specific expression, the existence of correspondence between esterase bands from spectra of different silkworm tissues and organs was suggested. Stage-specific expression of esterases in female genital glands, indicative of differentiated gene activity during ontogenesis, was established.

• Journal of The Korean Society of Grassland and Forage Science
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• v.11 no.3
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• pp.158-161
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• 1991

Horizontal starch gel electrophoresis, follow by enzyrne-specific staining, separate and visualize several legume esterase isozyme. Using extracts prepared from cotyledon, radicle and plumule of legume seedlings germinated 5 days. The results were as follows. 1. The number and staining intensity of esterase isozyme bands varies depending on the plant species. tissues and developmental stage. 2. Bands in the cotyledon of field bean seedling expressed 4 and 1 in radicle. 3. In soybean cultivars, cotyledon of IIwangkum-kong had 3 bands and 1 band in the examined tissues of Paldal-kong and Jangkyung-kong seedling. 4. The cotyledon and radicle of french bean seedling had 3 bands, respectively. 5. The highest esterase isozyme activity appears to be expressed in the cotyledon and radicle of french bean, as indicated by intensity of stain, with the Paldal-kong particulary active.

• Journal of the Korean Graphic Arts Communication Society
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• v.26 no.1
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• pp.17-28
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• 2008

The wood-pulp is treated with the three enzymes; Endo-xylanase, exo-xylanase and acetyl-esterase. The maximum value of relative activity appeared 0.95 in acetyl-esterase at $40^{\circ}C$, 0.9 in exo-xylanase at $40^{\circ}C$, and 0.8 in endo-xylanase at $50^{\circ}C$, respectively. And it has measured 0.8 in endo-xylanase, 0.95 in acetyl-esterase at pH 6 and 0.9 in exo-xylanase at pH 5, while the maximum value of relative activity does not rely on reaction time for three enzymes treatment, and the value was about 0.9, respectively. We have watched that decreased Kappa number and increased brightness. And it turned out that the three enzyme produced a lot of reducing sugar with wood-pulp treatment.

• Parasites, Hosts and Diseases
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• v.31 no.2
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• pp.165-168
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• 1993

In order to know the enzyme activities of Filbricola seouzenis, an intestinal trematode of human and rodent in Korea. the enzyme histochemical method is applicated. Activities of acid phosphatase (E.C.3.1.3.2) and non-specific esterase (E.C.3.1.1) were present in microvilli and glandular cells of trlbocytic organ and the epithelium of the caecum.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.542-548
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• 1993

Bacillus stearothermophilus was shown to express multiple xylanolytic enzymes including acetyl xylan esterase. Genomic DNA of the strain partially digested with HindIII was ligated into the HindIII site of pBR322, and expressed in E. coli HB101 cells in order to clone the gene for acetyl xylan esterase. One transformant among 4000 screened formed a clear zone around its colony on the LB agar supplemented with 1.0% tributyrin. The functional clone harbored the recombinant plasmid pKMG5 with an insert of 5.1kb.

• The Korean Journal of Zoology
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• v.31 no.2
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• pp.147-155
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• 1988

Six species of false spider mites were collected and ciassifled in South Korea. Among them, a taxonomic description was carried out on the following four species new to Korea: 1. Aegyptobia nothus Pritchard and Baker, 2. Pentomerismus taxi (Hailer), 3. P. oregonensis McGregor, 4. Brevipalpus lewisi McGregor. And also esterase and alkaline phosphatase patterns obtained by polyacrylamide slab gel electrophoresis were compared on some spades. Esterase rymogram showed difference among species in band number and mobility.

• The Korean Journal of Mycology
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• v.25 no.2 s.81
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• pp.85-90
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• 1997

The Isozyme activities of Lentinula edodes were studied as a preliminary study for genetic analysis after protoplast fusion. The presence of peroxidase, esterase, superoxide dismutase, acid phosphatase, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ was examined. An intracellular buffer-soluble protein from the mycelia was used for enzyme analysis on nondenaturing polyacrylamide gels. The auxotrophs of Lentinula edodes were positive for peroxidase, esterase, superoxide dismutase and acid phosphatase. However, alkaline phosphatase, alcohol dehydrogenase and ${\alpha}-amylase$ were not detected. The esterase and peroxidase were not affected by the various culture age. Isozyme identification may be a useful tool after protoplast fusion.

• Journal of Applied Biological Chemistry
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• v.51 no.3
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• pp.95-101
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• 2008

The gene encoding a putative esterase of Xanthomonas oryzae pv. oryzae was cloned using PCR technique. The gene was expressed with His6 tag in E. coli. One-step purification of the recombinant esterase with Ni-NTA resin resulted in one band by SDS-PAGE analysis. The purified enzyme showed a molecular weight of 30 kDa, as expected, therefore the enzyme was a mononer. The enzyme was the most active toward p-nitrophenyl (p-NP) acetate and p-NP-butyrate to a lesser extent. However, the enzyme could not hydrolyze p-NP-myristate, palmitate, and stearate. Therefore, the enzyme is considered as an esterase, very different from lipase. The purified esterase had optimal pH at around 8.0 and was stable in a broad range of pH values. The optimal temperature ranged from 30 to $40^{\circ}C$, and the residual activity observed after heat treatment at $55^{\circ}C$ for 20 min was 72 % of the initial activity. The activity was inhibited by the presence of copper and cobalt ions.

• Microbiology and Biotechnology Letters
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• v.25 no.1
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• pp.23-29
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• 1997

The nucleotide sequence of the estI gene encoding acetylxylan esterase I of Bacillus stearothermophilus was determined and analyzed. The estI gene was found to consist of a 810 base pair open reading frame coding for a polypeptide of 270 amino acids with a deduced molecular weight of 30 kDa. This was in well agreement with the molecular weight (29 kDa) estimated by SDS-PAGE of the purified esterase. The coding sequence was preceded by a putative ribo some binding site 10 bp upsteam of the ATG codon. Further 53 bp upstream, the transcription initiation signals were identified. The putative $_{-}$10 sequence (TCCAAT) and $_{-}$35 seqence (TTGAAT) corresponded closely to the respective consensus sequences for the Bacillus subtiis major RNA polymerase. The G+C content of the coding region of the estI was 51% whereas that of the third position of codone was 60.2%. The N-terminal amino acid sequence of the EstI deduced from the nucleotide sequence perfectly matched the corresponding region of the purified esterase described previously. Comparison with the amino acid sequence of other esterases and lipases reported so far allowed us to identify a sequence, GLSMG at positions 123 to 127 of the EstI which was reported to be the highly conserved active site sequence for those enzymes. The nucleotide sequence of the estI revealed 55.7% homology to that of the xylC coding for the acetylxylan esterase of Caldocellum saccharolyticum.