• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.255-262
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• 1992

In vitro digestibility of filefish, protein was substantially decreased by fiber constituents in the follow-ing order : pectin (9.97%), gum karaya (7.03%), sodium alginate (6.12%),and cellulose (1.52%). The order of reduction by fibrous residues from vegetables ranked as follows : sea tangle (12.36%), Ro-maine lettuce (11.12%), perillar leaf (8.96%), and green pepper (5.15%). The inhibitory effect of the dietary fibers towards filefish protein digestion, expressed as soybean trypsin inhibitor equivalents, in-creased with added levels, but the inhibition differed with the sources of dietary fibers. Sea tangle and sodium alginate were most active in decreasing the concentration of essential amino acid from filefish protein hydrolysis. Sodium alginate exerted an inhibitory effect on the activity of trypsin, but the other fiber constituents did not have an inhibitory potency on trypsin and bacterial pretense (Streptomyces griceus). Results supported that dietary fiber components may reduce protein digestibility through the interaction of dietary fiber components with filefish protein.

• Journal of Life Science
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• v.22 no.5
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• pp.627-633
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• 2012

$Microbulbifer$ sp. AJ-3 was used to acquire the degrading products from $Capsosiphon$ $fulvescens$ (DPCF), which were investigated to determine its physiological activities. A crude enzyme extract from $Microbulbifer$ sp. AJ-3 hydrolyzes polysaccharide substrates such as agar, agarose, alginic acid, fucoidan, laminaran, starch, and chitin. Among them, agarose, laminaran, and alginic acid showed higher activities, especially alginic acid. The antioxidant activity of DPCF was measured by using 2,2-diphenyl-1-picryl-hydrazyl (DPPH) and superoxide dismutase (SOD)-like activities and were about 32% and 93% at 2 mg/ml, respectively. In addition, the nitrite-scavenging activity of DPCF was about 82%, 53%, and 12% at pH levels of 1.2, 3.0, and 6.0, respectively. To determine the influence of DPCF on alcohol metabolism, the generating activity of reduced-nicotinamide adenine dinucleotide (NADH) by alcohol dehydrogenase (ADH) was measured. The facilitating rate of ADH activity by DPCF was 130% at 2 mg/ml. The tyrosinase inhibitory activity of DPCF was slightly increased in a dose-dependent manner and was about 28% at 2 mg/ml. These results indicated that the enzymatic products from DPCF have a strong antioxidant, nitrite scavenging, and alcohol metabolizing activity.

• Biotechnology and Bioprocess Engineering:BBE
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• v.10 no.1
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• pp.52-59
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• 2005

The study was targeted to saccharify foodwastes with the cellulolytic and amylolytic enzymes obtained from culture supernatant of Trichoderma harzianum FJ1 and analyze the kinetics of the saccharification in order to enlarge the utilization in industrial application. T. harzianum FJ1 highly produced various cellulolytic (filter paperase 0.9, carboxymethyl cellulase 22.0, ${\beta}$-glucosidase 1.2, Avicelase 0.4, xylanase 30.8, as U/mL-supernatant) and amylolytic (${alpha}$-amylase 5.6, ${\beta}$-amylase 3.1, glucoamylase 2.6, as U/mL-supernatant) enzymes. The $23{\sim}98\;g/L$ of reducing sugars were obtained under various experimental conditions by changing FPase to between $0.2{\sim}0.6\;U/mL$ and foodwastes between $5{\sim}20\%$ (w/v), with fixed conditions at $50^{\circ}C$, pH 5.0, and 100 rpm for 24 h. As the enzymatic hydrolysis of foodwastes were performed in a heterogeneous solid-liquid reaction system, it was significantly influenced by enzyme and substrate concentrations used, where the pH and temperature were fixed at their experimental optima of 5.0 and $50^{\circ}C$, respectively. An empirical model was employed to simplify the kinetics of the saccharification reaction. The reducing sugars concentration (X, g/L) in the saccharification reaction was expressed by a power curve ($X=K{\cdot}t^n$) for the reaction time (t), where the coefficient, K and n. were related to functions of the enzymes concentrations (E) and foodwastes concentrations (S), as follow: $K=10.894{\cdot}Ln(E{\cdot}S^2)-56.768,\;n=0.0608{\cdot}(E/S)^{-0.2130}$. The kinetic developed to analyze the effective saccharification of foodwastes composed of complex organic compounds could adequately explain the cases under various saccharification conditions. The kinetics results would be available for reducing sugars production processes, with the reducing sugars obtained at a lower cost can be used as carbon and energy sources in various fermentation industries.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.4
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• pp.635-641
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• 2000

In order to utilize the protein source from a fish proessing by-product, cod was hydrolyzed with various enzymes such as tuna pyloric caeca crude enzyme (TPCCE), a-chymotrypsin, trypsin, papain and pronase E. The TPCCE hydrolysate acquired the highest sensory properties on taste, odor and color. The resultant cod rfame protein hydrolysate (CFPH) which was hydrolyzed with TPCCE, was separated through a series of ultrafiltration membranes with molecular weight cut-off (MWCO) of 30, 10, 5 and 1 kDa, and four types of permeates in cluding 30 K (permeate from 30 kDa membrane), 10 K (permeate from 10 kDa membrane), 5 K (permeate from 5 kDa membrane) and 1 K (permeate from 1 kDa membrane) were obtained. The natural sauces were prepared with 30 K, 10 K, 5 K and 1 K hydrolysate, and the sauce prepared with 1 K hydrolysate was the best score in sensory evaluations. In addition the mixed sauce prepared with 1 K hydrolysate and commercial soy sauce was similar to commercial sauce in sensory properties. These results suggest that the mixed sauce would be utilized as the substitute of acid-hydrolysis sauce.

• Microbiology and Biotechnology Letters
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• v.41 no.3
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• pp.263-271
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• 2013

A xylanase-producing bacterium was isolated from a soil sample collected in Yongin city, Korea. The strain was aerobic and gram positive, and grew between pH 5.0 and 11.0, forming a yellow-colored colony. The strain was classified as a novel subspecies bacterium of Paenibacillus barcinonensis by 16S rRNA gene sequence similarity, phylogenetic analysis, phenotypic, and biochemical characteristics, and thus named Paenibacillus sp. HX-1. This strain produced extracellular endo-${\beta}$-1,4-xylanase, and the best xylanolytic activity (205.17 unit/ml) was obtained at 96 h in an optimized TNX medium containing 1% (w/v) bacto tryptone, 1% (w/v) NaCl, and 0.7% (w/v) beechwood xylan at pH 7.0, $37^{\circ}C$ and 200 rpm. The endo-${\beta}$-1,4-xylanase produced by the strain HX-1 yielded xylobiose as the end product from beechwood xylan hydrolysis. The enzyme exhibited optimum pH and temperature at pH 7.0 and $45^{\circ}C$, respectively. The remarkable enhancing effect of the TNX medium on xylanase production by HX-1, in spite of its simple formula, may have great advantages for industrial applications of xylanase.

• Journal of Animal Science and Technology
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• v.44 no.6
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• pp.801-808
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• 2002

Proteolytic activities of some commercial milk clotting enzymes(rennet, trypsin, pepsin, papain W-40, neutrase 1.5 and protease S) in bovine skim milk containing 0.02% $CaCl_2$ were determined by measuring DH(Degree of Hydrolysis), NPN(Non Protein Nitrogen) and by comparing patterns of SDS-PAGE(Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis). The DH of microbial enzymes(neutrase 1.5 and protease S) and trypsin in bovine skim milk were higher than those of pepsin and papain W-40. The amounts of NPN in the milk treated with trypsin and the other animal enzymes(rennet and pepsin) showed the highest and lowest degrees of proteolysis, respectively. SDS-PAGE showed that trypsin and protease S hydrolyzed $\alpha$-lactalbumin and papain W-40 hydrolyzed $\beta$-lactoglobulin slightly, while neutrase 1.5 hydrolyzed both $\alpha$-lactalbumin and $\beta$-lactoglobulin after treating for 90 min. Trypsin and protease S easily hydrolyzed ${\alpha}_s$-casein and $\beta$-casein, which were not hydrolyzed by rennet. Papain W-40 hydrolyzed $\kappa$-casein more than rennet as shown in SDS-PAGE. Based on the results of the experiments, the DH and NPN of trypsin, neutrase 1.5 and protease S were shown to be higher than those of the other enzymes. The SDS-PAGE patterns of papain W-40 and neutrase 1.5 were similar with that of rennet.

• Journal of the Korean Wood Science and Technology
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• v.39 no.3
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• pp.221-229
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• 2011

Due to the increase of oil price and the environmental issue such as the emission of volatile organic compounds, the necessity for developing alternative resins of petroleum-based adhesive resins, which have extensively been used for the manufacture of wood-based products, has been speculation since the early 1990. In our study, rapeseed flour (RSF), which is the by-product of bio-diesel produced from rapeseed, were hydrolyzed by enzymes. As a crosslinking agents of the RSF hydrolyzates, phenol-formaldehyde prepolymers (PF) were prepared. The RSF hydrolyzates and PF were mixed to complete the formulation of RSF-based adhesive resins, and the resins were applied to make the laminated veneer lumber (LVL). The physical and mechanical properties of the LVL were measured to examine whether RSF can be used as raw materials of adhesive resins for the fabrication of LVL or not. The average moisture content and soaking delamination rate of the LVL bonded with RSF-based adhesive resins exceeded the minimum requirement of KS standard. Moreover, thermal analysis of the RSF-based resins showed similar tendencies except for the RSF-based adhesive resins formulated with pectinase-hydrolyzed RSF. The bending strengths of the LVL were higher than that of the LVL made with commercial PF resins. These results showed the potential of RSF as a raw material of alternative adhesives for the production of LVL. Further works on the optimal conditions of RSF hydrolysis and spreading characteristics for RSF-based adhesive resins is required to improve the adhesive performance of RSF-based resins.

• Korean Journal of Food Science and Technology
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• v.50 no.2
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• pp.132-137
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• 2018

Enzymatic treatments of maize flour (MF) were investigated using commercial carbohydrases (Ultraflo L and Pentopan 500 BG) to enhance the phenolic acid content and antioxidant property. The total phenolic acid content of the MF was 3.76 mg/100 g, whereas those of the Pentopan 500 BG and Ultraflo L treated MF were 6.85 and 39.55 mg/100 g, respectively. Particularly, ferulic acid content of Pentopan 500 BG-treated MF was 20.0 times higher than that of untreated MF (1.7 vs. 33.9 mg/100 g). Pentopan 500 BG appeared to be more effective than Ultraflo L in increasing the free phenolic acid content. Antioxidant activities of enzyme treated MF were significantly higher than untreated MF. In particular, the Pentopan 500 BG-treated MF (16.0 mmol TE/100 g) was approximately 1.5 times higher than untreated MF (12.6 mmol TE/100 g). Enzymatic hydrolysis of cell wall polysaccharides in MF could be used as an effective procedure for not only increasing phenolic content but also antioxidant activities.

• Korean Journal of Microbiology
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• v.44 no.3
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• pp.264-269
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• 2008

To develop an amylolytic industrial yeast strain producing $\beta$-amylase, the BAMY gene encoding Achlya bisexualis $\beta$-amylase was constitutively expressed under the control of the alcohol dehydrogenase gene promoter (ADC1p) in an industrial strain of Saccharomyces cerevisiae. Yeast transformation was carried out by an integration system containing $\delta$-sequences as the recombination site. The integrative cassette devoid of bacterial DNA sequences was constructed that contains the BAMY gene and $\delta$-sequences. Industrial S. cerevisiae transformed with this integrative cassette secreted 45 kDa $\beta$-amylase into the culture medium. The $\beta$-amylase activity of the transformant was approximately 18.5-times higher than that of A. bisexualis. The multi-integrated BAMY genes in the transform ant were stable after 100 generations of growth in nonselective medium. Hydrolysis of soluble starch and various starches with the enzyme released maltose but not glucose or oligosaccharides.

• Journal of Life Science
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• v.8 no.4
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• pp.410-415
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• 1998

Procine pepsin hydrolysis of hexapeptide L-S-pNF-Nle-A-OMe in the presence of dipeptide L-L generates a new peak on HPLC analysis of reaction mixtures that is not seen when enzyme is incubated with either peptide alone. The peaks can be detected spectroscopically at either 214 or 254 nm, the latter consistent with a new peptide containing the p-nitro-F residue. The data suggest acyl transpeptidation between E(L-S-pNF) and L-L to form L-S-pNF-L-L. Consistent with this inference are (1) the ability of L-L-NH$_{2}$ and inability of Boc-L-L to undergo a similar transpeptidation reaction, and (2) the data from electrospray mass spectrum. This synthesis requires that Nle-A-L-OMe be released before L-S-pNF, an order opposite to that proposed on the basis of product inhibition kinetics. Consistent with this inference are reciprocal solvent isotope effects ; normal isotope effects of 1.736$\pm$0.121 on the formation of Nle-A-L-OMe and 2.281$\pm$0.184 in the formation of L-S-pNF, coupled to an inverse isotope effects of 0.576$\pm$0.045 on the formation of L-S-pNF-L-L. Because transpeptidation precedes faster in D$_{2}$O, the isotopically-sensitive step must occur after release of Nle-A-L-OMe. Isotopically-enhanced transpeptidation is consistent with the Uni-Bi iso memchanism postulated on the basis of an isotope effects on Vmax but not on Vmax/Km$^{1)}$ and confirmed by isotope effects on the onset of inhibition by pepstatin$^{2)}$.