• Korean Journal of Food Science and Technology
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• v.27 no.6
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• pp.964-971
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• 1995

Volatile flavor compounds and free amino acids in untreated and hydrolysate pen shell by-product produced with APL 440 protease were compared by vacuum simultaneous steam distillation-solvent extraction/gas chromatography/mass spectrometry. A total of 109 volatile flavor compounds were detected in hydrolysate (65 compounds) or the 109 volatile flavor compounds were detected in untreated pen shell by-product (88). These compounds were composed of aldehydes(16), ketones(17), alcohols(31), nitrogen containing compounds (16), aromatic hydrocarbon compounds(8), esters(3), and miscellaneous compounds (17). Levels of aldehydes and aromatic hydrocarbons decreased after hydrolysis, whereas levels of nitrogen containing compounds increased 3 times than in untreated pen shell by-product. Taurine, known to be having a physiological function, was accounted for 31.25% of total amino acids in hydrolysate.

• Applied Chemistry for Engineering
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• v.23 no.6
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• pp.599-603
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• 2012

The enantioselective hydrolysis of racemic styrene oxide in organic solvents was conducted using a recombinant E. coli expressing protein-engineered Mugil cephalus epoxide hydrolase (McEH). The volumetric total activity of the recombinant E. coli was enhanced 2.2-fold by IPTG induction at a mid-exponential growth phase. Among organic solvents with different log P values, isooctane was chosen based on the high activity and the enantioselectivity of McEH. Some lyoprotectants such as skim milk or sucrose enhanced the McEH activity. Enantiopure (S)-Styrene oxide with a 98% ee was obtained from the racemic styrene oxide with a 53.6% yield based on its theoretical yield in isooctane.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.2
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• pp.120-132
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• 1993

A continuous hollow fiber membrane reactor(CHFMR) was developed and optimized for the production of yellowfin sole(Limanda aspera) skin gelatin hydrolysates using trypsin. The results were summerized as follows: The $K_m$ value of the CHFMR was 2.4 times higher than that of the batch reactor, indicating reduced enzyme affinity for the substrate. The $K_2$ value of the CHFMR was 8.5 times lower than that of the batch process, showing a significant reduction in trypsin activity in the CHFMR. The optimum operating conditions for the CHFMR process were $55^{\circ}C$, pH 9.0, flux 7.79 ml/min, residence time 77min, and trypsin to substrate ratio, 0.01(w/w) After operating for 60min under the above conditions, $79\%$ of the total amount of initial gelatin was hydrolysed. Enzyme leakage was observed through the 10,000 MWCO membrane after the 20min of reactor operation, while none occurred after 5hr. Total enzyme leakage was about $12.95\%$ at $55^{\circ}C$ for 5hrs. However, there was no apparent correlation between enzyme leakage and substrate hydrolysis. The membrane has a significant effect on trypsin activity loss for 60min of the CHFMR operation. The CHFMR operating with the membrane lost $34\%$ of the initial activity versus a $23\%$ loss of activity after 3hr in the continuous reactor lacking the hollow fiber membrane. The measurement of fouling property showed that relative flux reduction was $91\%$ and flux recover rate was $92\%$ at $10\%$ substrate solution. The productivity(378.85mg product/mg enzyme) of the CHFMR was more than 4 times higher than that of the batch reactor at $55^{\circ}C$.

• Journal of Applied Biological Chemistry
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• v.51 no.6
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• pp.272-276
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• 2008

Purification and some properties of Xylogone sphaerospora ${\beta}$-mannanase were reprevious previous paper. Locust bean gum galactomannan was hydrolyzed by the purified ${\beta}$-mannanase, and then the hydrolysates was separated by activated carbon column chromatography. The main hydrolysates were composed of D.P. (Degree of Polymerization) 4 and 6 galactosyl mannooligosaccharides. For elucidate the structure of D.P 4 and 6 galactosyl mannooligosaccharides, sequential enzymatic action was performed. D.P 4 and 6 were identified as ${Gal^2}{Man_3}\;(6^2-mono-O-{\alpha}-D-galactopyranosyl-4-O-{\beta}-D-mannotriose)$ and ${Gal^2}{Man_5}\;(6^2-mono-O-{\alpha}-D-galacto- pyranosyl-4-O-{\beta}-D-mannopentaose)$. To investigate the effects of locust bean gum galactosyl mannooligosaccharides on in vitro growth of Bifidobacterium longum, B. bifidum, B. infantis, B. adolescentis, B. animalis, B. auglutum and B. breve. Bifidobacterium spp. were cultivated individually on the modified-MRS medium containing carbon source such as D.P. 4 and D.P. 6 galactosyl mannooligosaccharides, respectively. B. longum and B. bifidum grew up to-fold and 6.6-fold more effectively by the treatment of D.P. 6 galactosyl mannooligosaccharides, compared to those of standard MRS medium. Especially, D.P. 6 was more effective than D.P. 4 galactosyl mannooligosaccharide on the growth of Bifidobacterium spp.

• Proceedings of the Korean Society of Dyers and Finishers Conference
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• 2004.11a
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• pp.265-269
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• 2004

• Journal of the Korean Society of Food Science and Nutrition
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• v.33 no.7
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• pp.1186-1191
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• 2004

Bacillus sp. $\beta$-mannanase was purified by DEAE-sephadex ion exchange column chromatography. The partially purified P-mannanase exhibited maximum activity at pH 6.0 and 5$0^{\circ}C$, and was stable at a pH range of 5.5 to 7.0, and at temperature between 30 to 5$0^{\circ}C$. Konjac glucomannan was hydrolyzed by the purified $\beta$-mannanase, and then hydrolysates separated by 1st activated carbon column chromatography and 2nd sephadex G-25 gel filtration. The main hydrolysates were composed of D.P 5 and 7 glucomannooligosaccharides by TLC and FACE method. To investigate the effects of guar gum glucomannooligosaccharides on the in vitro growth of B. longum, B. bifidum, B. infantis, B. adolescentis, B. animalis, and B. breve, Bifidobacterium spp. were cultivated individually on the modified-MRS medium containing carbon SOUTce such as D.P 5, and D.P 7 glucomannooligosaccharides, respectively. B. longum grew up 4.6-fold and 5.3-fold more effectively by the replacement of D.P 5 and 7 glucomannooligosaccharides as the carbon source in a comparasion of standard MRS. Also, B. breve and B. animalis slightly grew up by the treatment of D.P 5 glucomannooligosaccharide.

• Microbiology and Biotechnology Letters
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• v.18 no.4
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• pp.437-441
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• 1990

For the genetic development of more powerful antagonistic Pseudomom - YPL-1 as a biocontxol agent against soilborne plant pathogenic Fuaarium solani causing root rot of many important crops, mutants improving the productivity of chitinase were obtained by mutation with UV radiation or NTG treatment, P. stutzeri YPL-M26 (UV mutant) and P. stutzeri YPL-MI78 (NTG mutant) could improve the productivity of chitinase by 2.5 and 2.0 times, and its antifungal activity by 1.7 and 1.5 times, respectively. The antifungal mechanism of P. stutzeri YPL-M26 was caused by lysis of the fungal cell wall by hydrolytic enzymes such as chitinase. The antifungal activity of crude chitinase of P. stutzeri YPLM26 on the mycelial growth of F. solani was observed to be much higher than that of the original strain. The enzymes produced by P. stutzeri YPL-M26 were the same as the original strain in enzymatic properties such as optimal pH and temperature.

• Korean Journal of Microbiology
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• v.40 no.4
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• pp.328-333
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• 2004

The maximum productivity of ${\alpha}-galactosidase,$ capable of hydrolyzing completely ${\alpha}-D-l,6-galactopyranosyl$ linkages within oligomeric substrates such as melibiose, raffinose and stachyose to liberate galactose residue, was reached to 718 mU/ml in the culture filtrate of Bacillus licheniformis at death phase. The ${\alpha}-galactosidase$ was identified to show different efficiencies for hydrolyzing the ${\alpha}-galactooligosaccharides$ according to analysis of reaction products by both TLC and quantification of the liberated reducing sugars. The enzyme was active on ${\alpha}-galactooligosaccharides$ in the order of melibiose, raffinose, and stachyose. Though the hydrolyzing activity of enzyme was faintly inhibited by reaction products such as galactose, glucose and sucrose with amounts of five folds more than the added substrates (20 mM), the largest inhibition of enzyme activity was caused by galactose among the end products. Unknown compound, which migrated slower than melibiose on TLC, was detected during hydrolysis reaction of melibiose, suggesting that the ${\alpha}-galactosidase$ has a glycosyl transferase activity. In addition, the enzyme was able to hydrolyze efficiently raffinose and stachyose existed in the soluble extract of soybean meal.

• Korean Journal of Food Science and Technology
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• v.27 no.5
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• pp.708-715
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• 1995

Effect of enzymatic modification with pepsin, papain and trypsin was studied on functional properties of isolated sesame meal protein hydrolysates. Solubility of protein hydrolysates distinctively increased from 2% to $53{\sim}94%$ at pH 4. Emulsifying properties showed marked increase 6 fold and 4.5 fold at degree of 10%, 20% hydrolysis by trypsin and degree of 10% hydrolysis by papain. The emulsion stability of the protein was unstable by heat treatment for 30 min. at $80^{\circ}C$. Foaming properties were also enhanced by enzymatic hydrolysis except at degree of 30% hydrolysis. Bulk density and water absorption of protein with trypsin and papain decreased about 0.1 g/ml and $0.3{\sim}0.7\;ml/g$, but oil absorption was increased about 1 ml/g.

• Journal of the Korean Chemical Society
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• v.40 no.4
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• pp.254-263
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• 1996

Five cobalt(Ⅲ) complexes were synthesized from bi- or tridentate nitrogen ligands. Catalytic actions of these complexes for hydrolyses of p-nitrophenyl picolinate, p-nitrophenyl nicotinate, and p-nitrophenyl isonicotinate were investigated by a spectrophotometric method. p-Nitrophenyl picolinate showed the most senstive reaction among three substrates by these catalysts. Aquohydroxo Co(Ⅲ) complexes raised as much as 21∼40 times the rate of hydrolysis of p-nitrophenyl picolinate at pH 6.5. Activities of complexes were in the order: Co(ibpn)(OH)2(OH2) > Co(aepn)(OH)2(OH2) > Co(tn)2(OH)(OH2) > Co (bpy)2(OH)(OH2) > Co(dien)(OH)2(OH2). Catalytic hydrolysis was postulated to proceed through a intramolecular general base catalysis path which is mixed by a partial intramolecular nucleophilic catalysis.