• Microbiology and Biotechnology Letters
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• v.18 no.3
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• pp.251-259
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• 1990

Asp. usumii IAM 2185 was selected as a strain producing the powerful raw starch digesting glucoamylase. The optimum initial pH, the optimum temperature and the optimum cultural time for the enzyme production on wheat bran medium were pH 6-8,25-$30^{\circ}C$ and 72 hrs, respectively. The addition of ammonium nitrate and albumin on wheat bran medium, respectively, increase slightly the enzyme production. The enzyme was purified by ammonium sulfate fractionation, CM-cellulose and DEAE-cellulose column chromatography. The specific activity of the purified enzyme was 34.3 U/mg protein and the yield of enzyme activity was 10.3%. The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis and its molecular weight was estimated to be 67,000 by SDS polyacrylamide disc gel electrophoresis. The isoelectric point for the purified enzyme was pR 3.7. The optimum temperature and optimum pH were $60^{\circ}C$and pH 3.0 and the purified enzyme was stable in the pH range of 1.0-11.0. The purified enzyme was stable below $50^{\circ}C$ and its thermostability was greatly increased by the addition of $Ca^{2+}$. The purified enzyme showed a high hydrolysis rate on various raw starches such as corn, rice, yam, arrow root, sweet potato and glutinous rice.

• Microbiology and Biotechnology Letters
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• v.20 no.4
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• pp.409-416
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• 1992

The optimum cultural temperature and time for the pullulanase production by Bacillus cereus were $15^{\circ}C$ and 72 hrs, respectively. The addition of casein, nutrient broth and egg albumin to the basal medium, respectively, increased greatly the enzyme production. The enzyme was purified by ammonium sulfate fractionation, CM-cellulose and DEAE-cellulose column chromatographies. The specific activity of the purified enzyme was 29.09 U/mg protein and the yield of enzyme activity was 17.1% The purified enzyme showed a single band on polyacrylamide disc gel electrophoresis and its molecular weight was estimated to be 61,000 by SDSpolyacrylamide disc gel electrophoresis. The isoelectric point for the purified enzyme was pH 7.0. The optimum temperature and pH were $40^{\circ}C$ and 6.5. The purified enzyme was stable below $35^{\circ}C$ and in the pH range of 6.5-11.0. It was greatly inhibited by $Ag^{+}$, $Hg^{2+}$ and $Zn^{2+}$, and its thermal stability was increased by the addition of $Ca^{2+}$ Among various substrates, pullulan was favorably hydrolyzed by the purified enzyme and the hydrolysis product 011 pulluIan was maltotriose.

• Applied Chemistry for Engineering
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• v.16 no.2
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• pp.267-274
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• 2005

Preparation of cellulose type underwater non-segregation admixture was attempted and the hardening characteristics of underwater concrete according to the addition of this admixture was investigated in order to make underwater concrete with the compressive strength ratio of 0.8 to that of concrete manufactured in common atmosphere. The proposed underwater non-segregation admixture consisted of methyl cellulose of 0.4% by weight, silicon type antifoaming agent of 20% by weight, and sodium aluminate of 0.1% by weight to the amount of cement as setting accelerant, respectively. As the proposed non-segregation admixture was increased, the amount of suspended solid decreased, air content in concrete was increased but the flow loses by elapsed time did not change. The proper amount added of the proposed non-segregation adimixture was 0.8 wt% to the amount of cement. The compressive strength of the test sample underwater concrete manufactured by the addition of the proposed admixture was $325Kg/cm^3$, and the ratio of compressive strength of this sample concrete to that of a concrete manufactured in air was 0.94.

• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.322-328
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• 1984

These experiments were conducted to purify the glucoamylase produced by Rhizopus oryzae. Two forms of glucoamylase (GI and GII) from Phizopus oryzae were purified by $(NH_2)_2SO_4$ fractionation, acetone fractionation and successive column chromatography on DEAE-cellulose and CM-cellulose. The specific activities of GI and GII toward soluble starch were 157.6 U/㎎. protein (37.5 fold of crude extract), and 164.7 U/㎎. protein (39.2 fold of curde extract), respectively, and the yields of them were 4.3% and 3.8%, respectively. The two purified enzymes have shown a single band by polyacrylamide disc gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The protein bands of their electrophoresis gel were revealed to have glucoamylase activity by iodine staining and were proved to be glycoprotein by periodic acid Schiff's staining.

• Journal of Sericultural and Entomological Science
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• v.28 no.1
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• pp.30-36
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• 1986

Polyacrylamide gel electrophoresis and autoradiography were applied to investigate the developmental profiles of the major hemplymph proteins (MHPs) and their biosynthesis. In addition, some biochemical methods were also used to isolate and purify the MHPs. The obtained results are summarized as follows. 1. MHP-a began to appear from the 2nd day of the fourth-instar larva while MHP-b and -c were detected first on the 1st day of the fifth-instar larva. All these proteins, however, showed a drastic increase in concentration at the 2nd day of the fifth-instar larva. 2. MHP-b and -c were synthesized in fat body on early day of the fifth-instar larva, but the possibility of MHP-a synthesis in fat body was excluded. 3. MHP-b was isolated and purified by heat-treatment (6$0^{\circ}C$), gel filtration on Sephadex G-100 and column chromatography on DEAE-cellulose and CM-cellulose. Purified MHP-b showed a single band on polyacrylamide gel- and SDS-polyacrylamide gel electrophoresis.

• Korean Journal of Food Science and Technology
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• v.18 no.4
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• pp.270-277
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• 1986

Ficin, a proteolytic enzyme in Fig latex, was extracted and purified with using ammonium sulfate and CM-cellulose column chromatography, respectively, and studied for its chemical properties. The disc gel electrophoresis showed one major and three minor bands for $(NH_4)_2SO_4$ extract and only one band showed after CM-cellulose chromatography. The optimum conditions for ficin activity was found to be pH 7.0 and $50^{\circ}C$. The amino acids composition of the purified ficin were 21.8% as acidic, 3.5% as basic and 74.7% as neutral amino acids. The amino acids analysis indicated that the ficin was composed of 174 amino acids residue having molecular weight of 19,500.

• Journal of the Korean Wood Science and Technology
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• v.52 no.3
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• pp.205-220
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• 2024

Various polylactic acid (PLA) blends were reinforced with untreated or silane-treated micro-sized cellulose fiber (MCF), successfully prepared as 3D printing filaments and then printed using a fused filament fabrication (FFF) 3D printer. In this study, we focused on developing 3D-printed MCF/PLA composites through silane treatment of MCF and investigating the effect of silane treatment on the various properties of FFF 3D-printed composites. Fourier transform infrared spectra confirmed the increase in hydrophobic properties of silane-treated MCF by showing the new absorption peaks at 1,100 cm^-1, 1,030 cm^-1, and 815 cm^-1 representing C-NH₂, Si-O-Si, and Si-CH₂ bonds, respectively. In scanning electron microscope images of silane-treated MCF filled PLA composites, the improved interfacial adhesion between MCF and PLA matrix was observed. The mechanical properties of the 3D-printed MCF/PLA composites with silane-treated MCF were improved compared to those of the 3D-printed MCF/PLA composites with untreated MCF. In particular, the highest tensile and flexural modulus values were observed for S-MCF10 (5,784.77 MPa) and S-MCF5 (2,441.67 MPa), respectively. The thermal stability of silane-treated MCF was enhanced by delaying the initial thermal decomposition temperature compared to untreated MCF. The thermal decomposition temperature difference at T₉₅ was around 26℃. This study suggests that the effect of silane treatment on the 3D-printed MCF/PLA composites is effective and promising.

• Journal of Food Hygiene and Safety
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• v.14 no.3
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• pp.233-237
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• 1999

The bacteriocin produced by Lactobacillus sp. GM7311 was purified by sequential steps including n-propanol/acetone treatment, CM-cellulose chromatography, and gel filtration on Sephacryl HR-100. The relative activity of bacteriocin increased 493-fold after final purification step with a recovery of 8.3%. Two protein bands of ca. 8,200 and 2,500 were detected by SDSPAGE of bacteriocin purified through CM-cellulose and sephacryl HR-100 chromatography and both of them had bacteriocin activity.

• Journal of the Korean Society of Safety
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• v.15 no.4
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• pp.95-100
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• 2000

This study was performed in Hartmann type dust explosion apparatus in order to research the dust explosion characteristics of hydroxypropyl methyl cellulose(HPMC): minimum explosive limit, minimum ignition energy, limiting oxygen concentration, maximum explosion pressure, rate of pressure rise, etc. The samples of HPMC dust were distributed into 120-140 mesh, 170-230 mesh and 325 under, and the gap distance of the discharge electrode was setted up at 5mm. The experimental results were obtained as follows: (1) The minimum explosive limit for HPMC dust was founded at 180g/㎥. the minimum ignition energy at 9.8mJ and the limiting oxygen concentration at 12%. (2) The maximum explosion pressure of HPMC dust was $8.1kg/cm^2\;{\cdot}\;$abs at the concentration of $500g/m^3$ and the maximum rate of pressure rise was 203.98 bar/sec at the concentration of $480g/m^3$ for 325 under.

• Journal of Life Science
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• v.22 no.7
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• pp.912-919
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• 2012

A Bacillus sp. strain producing celluase and xylanase was isolated from environmental soil with LB agar plate containing carboxymethylcellulose (CM-cellulose) and beechwood xylan stained with trypan blue as substrates, respectively. Based on the 16S rRNA gene sequence and API 50 CHL test, the strain was identified as B. subtilis and named B. subtilis NC1. The cellulase and xylanase from B. subtilis NC1 exhibited the highest activities for CM-cellulose and beechwood xylan as substrate, respectively, and both enzymes showed the maximum activity at pH 5.0 and $50^{\circ}C$. We cloned and sequenced the genes for cellulase and xylanase from genomic DNA of the B. subtilis NC1 by the shot-gun cloning method. The cloned cellulase and xylanase genes consisted of a 1,500 bp open reading frame (ORF) encoding a 499 amino acid protein with a calculated molecular mass of 55,251 Da and a 1,269 bp ORF encoding a 422 amino acid protein with a calculated molecular mass of 47,423 Da, respectively. The deduced amino acid sequences from the genes of cellulase and xylanase showed high identity with glycosyl hydrolases family (GH) 5 and 30, respectively.