• Journal of the Korean Wood Science and Technology
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• v.40 no.2
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• pp.123-132
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• 2012

Pre-pulping extracts were found to contain a dilute amount of xylo-oligosaccharides and acetic acid as the major components, and many minor components including other organic acids, lignin-derived phenolics, and sugar degradation products. Once separated from the pulp, a secondary hydrolysis step was required to hydrolyze oligomeric hemicellulose sugars into monomeric sugars before fermentation. The following study detailed the extent of hemicellulose recovery by pre-pulping using hot water extraction and characterized the hydrolysis of the extract with respect to comparing acid and enzymatic hydrolysis. The secondaryhydrolysis of hot water extracts made at an H-Factor of 800 was tested for a variety of acid and enzyme loading levels using the sulfuric acid and xylanases. The maximum fermentable sugar yield from acid and enzyme hydrolysis of the extract was 18.7 g/${\ell}$ and 17.7 g/${\ell}$ representing 84.6% and 80.1% of the maximum possible yield, respectively.

• Bulletin of the Korean Chemical Society
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• v.26 no.12
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• pp.1911-1920
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• 2005

Effective artificial metalloproteases have been designed by using cross-linked polystyrene as the backbone. Artificial active sites comprising Cu(II) complexes as the catalytic site and other metal centers or organic functionalities as binding sites were synthesized. The activity of Cu(II) centers for peptide hydrolysis was greatly enhanced on attachment to polystyrene. By placing binding sites in proximity to the catalytic centers, the ability to hydrolyze a variety of protein substrates at selected cleavage sites was improved. Thus far, the most advanced immobile artificial proteases have been obtained by attaching the aldehyde group in proximity to the Cu(II) complex of cyclen.

• KSBB Journal
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• v.16 no.3
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• pp.246-252
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• 2001

We isolated a bacterium that produces an extracellular maltopentaose(G5)-forming amylase from amylose and soluble starch. The bacterium was identified and assigned as a Bacillus sp. AIR-5. The amylase did not hydrolyze maltose, maltotriose, maltotetraose or maltopentaose. Optimum medium composition for maltopentaose production in flask culture was 2%(w/v) soluble starch, 0.4%(w/v) tryptone, 0.5%(w/v) NaCl, 0.5%(w/v) K$_2$HPO$_4$, and 3 mM CaCl$_2$at pH 8.0, 28$^{\circ}C$. The highest yield for maltopentaose production in this condition was 6.45 g/L and was 32.55% of theoretical yield.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.435-438
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• 2003

Epoxide hydrolase(EH) catalyze the enantioselective hydrolysis of racemic epoxides to corresponding diols. A recombinant Pichia pastoris with EH from Rhodotorula glutinis has been constructed by reverse transcriptase-polymerase chain reaction(RT-PCR). The recombinant biocatalyst enantioselectively hydrolyze (R)-styrene oxide faster than (S)-enantiomer. The catalytic activity of recombinant biocatalyst was 7-fold higher than that of wild-type strain. The recombinant EH biocatalyst can be used for kinetic resolution for the production of enantiopure styrene oxide.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.571-575
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• 2003

A marine aerobic Gram-negative bacterium, Pseudoalteromonas carrageenovora, has been blown to hydrolyze carrageenans, the sulfated galactans of red algae, and to desulfate oligo kappa-carrageenans. Recently, the gene encoding arylsulfatase (aryl-sulfate sulfohydrolase, E.C.3.1.6.1) of A. carrageenovora was cloned and the nucleotide sequence was reported. Enzymatic hydrolysis of sulfate groups in agaropectin simplifies the process of agarose preparation. In order to overproduce the enzyme, the arylsulfatase gene (astA, 984 bp ORF) from P. carrageenovora genome was amplified by PCR and subcloned into the pET21a vector. When the constructed plasmid pAST-A1 was introduced into E, coli BL21(DE3), the transformant on LB plate containing IPTG showed the hydrolyzing activity for p-nitrophenyl sulfate. Most of arylsulfatase activity was found in the cell lysate, but at $50\;{\sim}\;5000\;{\mu}M$ IPTG concentration the activity was found both in the culture supernatant and the cell lysate. The molecular weight of the recombinant enzyme was estimated to be 34 kDa by SDS-PAGE.

• Journal of the Korean Society of Food Science and Nutrition
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• v.20 no.1
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• pp.35-39
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• 1991

Properties of a protease purified from Neungee[Sarcodon aspratus(Berk, ) S. Ito] have been investigated. The enzyme displays a glycosylated serine protease. The enzyme is able to hydrolyze alanine glycine methionine glutamine and cysteine of N-CBZ and N-t-BOC-L-amino acid derivatibes relatively strongly but splits valine proline and isoleucine derivatives with low affinity which means the enzyme has the broad substrate spectrum toward the amino acids. Interestingly the enzyme was inhibited by bromelain inhibitor. That is the active site environ-ment of the enzyme is believed to be similar to that of bromelain However peptide mapping studies show that the two enzymes have distinct different cleavage sites.

• BMB Reports
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• v.28 no.2
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• pp.94-99
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• 1995

The properties of binding sites in the active site of $Zn^{2+}$-glycerophosphocholine cholinephosphodiesterase were examined using substrates and inhibitors of the enzyme. Phosphodiesterase hydrolyzed p-nitrophenylphosphocholine, p-aminophenylphosphocholine, and glycerophosphocholine, but did not hydrolyze either acylated glycerophosphocholine or bis (p-nitrophenyl)phosphate, suggesting a size limitation for interaction with a glyceryl moiety-binding subsite. The hydrolysis of p-nitrophenylphosphocholine was competitively inhibited by glycerophosphocholine and p-aminophenylphosphocholine, while glycerophosphoethanolamine was a weak inhibitor. The enzyme was also inhibited by choline, but not by ethanolamine. Thiocholine, a much more potent inhibitor than choline, was more inhibitory than cysteamine, suggesting a strict specificity of an anionic subsite adjacent to a $Zn^{2+}$ subsite. Of all oxyanions tested, the tellurite ion was found to strongly inhibit the enzyme by binding to a $Zn^{2+}$ subsite. The inhibitory role of tellurite was synergistically enhanced by tetraalkylammonium salts, but not by glycerol. Deactivation of the enzyme by diethylpyrocarbonate was partially protected by choline, but not by glycerophosphate. It is suggested that the active site of phosphodiesterase contains three binding subsites.

• Korean Journal of Pharmacognosy
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• v.30 no.4
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• pp.409-412
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• 1999

The in vitro anticoagulant and fibrinolytic activities of crude extract from insects which have been used as traditional medicines. The extracts of Formica, Huechys and Eupolyph-aga/Steleophaga prolonged activated partial thromboplastin time and thrombin time compared to the value of the control. The fibrinolytic activity of insect extracts was also tested by fibrin plate method. We found that the extracts of Cicadae Periostracum, Eupolyphaga/Steleophdga, Mantidis $O{\ddot{o}}otheca$ and Huechys directly could hydrolyze the fibrin clot without the activation of plasminogen by plasminogen activators.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.576-579
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• 1998

Water extract of mulberry tree barks(Morus alba Linne) was studied for its proteolytic activity. Protein content of the extract was 1.12mg/ml and its specific activity was 5.14U/ml. The enzyme was active on various proteins : the relative acitities were 100 for casein, 63 for albumin, 58 for collagen, 45 for hemoglobin and 36 gelatin, respectively. There suggested that the ability of the enzyme to hydrolyze meat was relatively high since those are major meat proteins. Optimum pH and temperature for proteolytic activity were : pH 6.0 and 6$0^{\circ}C$. And the enzyme was stable at the pH range of 6.0 to 7.0 and temperature between 50 and 8$0^{\circ}C$. Apparent proteolytic activities could support some scientific grounds of traditional application of mulberry tree barks to home cooking for meat tenderization.

• Journal of Microbiology and Biotechnology
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• v.8 no.1
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• pp.49-52
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• 1998

A fungal strain able to produce filter paper activity (FPase) was isolated from soil by testing the ability to hydrolyze using filter paper. The isolated strain was identified as an Aspergilus sp. judging from its morphological and microscopical characteristics. The cellulase-xylanase system of Aspergillus sp. 8-17 was detected in situ after gel electrophoresis in the presence of SDS and showed that each protein pattern had a distinct polypeptide composition. ${\beta}$-1,4-Glucanase, cellobiohydrolase, and xylanase activity profiles differ from protein patterns. The Aspergillus sp. 8-17 hydrolytic enzymes responsible for the hydrolysis of ${\beta}$-glucan, MUC, and xylan have multiple active forms.