• 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.

• Applied Biological Chemistry
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• v.34 no.1
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• pp.54-60
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• 1991

Serratia marcescens CK-3, decomposing chitin which is a mar component of cell wall in phyitopathogenic fungi, was isolated from the continuous cropping rhizosphere of pepper and cucumber and its enzymatic property was examined. S. marcescens CK-3 was found tn have an tagonistic effects against, Fusarium axysporum and Rhizoctonia solani and to have complex enzyme system such as chitinase, laminarinase, and proteinase. The preferable composition of the medium for production of chitinase was fond and was as follows : colloidal chitin 1.5%, tryptone 0.5%, glucose 1.0%, peptone 0.2%, $MgSO_4{\cdot}7H_2O\;0.1%,\;K_2HPO_4\;0.1%,\;and\;NaCl\;0.1%$(w/v), pH 6.8. The maximum enzyme production was observed after culture of 72 hours at $30^{\circ}C$ using a medium containing the above chemical composition. The optimal pH and temperature for in vitro activity of chitinase from S. marcescens CK-3 were pH 7.5 and $50^{\circ}C$, respectively. The enzyme activity in-creased by metal ions such as$Ag^+$ and $Mn^{++}$.

• Korean Journal of Food Science and Technology
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• v.51 no.4
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• pp.348-355
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• 2019

This study investigated the impact of cellulase treatment on the extraction yield of potato starch (PS), and compared the physicochemical properties of PS by conventional (CSE) and enzymatic (ESE) starch extraction. In ESE, the PS extraction yield was predominantly influenced by reaction temperature, time and their interaction, compared to the cellulase concentration. When potatoes were treated for 8 h at $40^{\circ}C$ with 1.5% cellulase, the PS extraction yield was about 3.4-fold higher than that by CSE. Compared to CSE-PS, ESE-PS showed lower total starch contents and higher amylose contents, resulting in lower swelling factors and distorted pasting viscosity profiles accompanied by absence of peak and breakdown viscosities. However, ESE did not affect the gelatinization characteristics of PS. Overall results suggested that ESE can provide the highest yield of PS, and ESE-PS can be a potential starch source for extending the utilization of PS in food industries.

• Journal of Microbiology and Biotechnology
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• v.4 no.2
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• pp.113-118
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• 1994

A bacterial strain NS-83 isolated from soil was able to produce an extracellular thermostable protease. The strain was identified as Pseudomonas aeruginosa based on its morphological and physiological characteristics. A thermostable protease from this strain has been purified to homogeneity as judged by SDS-PAGE and isoelectric focusing. The purification procedures included hydrophobic interaction, ion exchange, and gel filtration chromatography. The $M_r$ and the pl of the enzyme were 32,000 and 5.9, respectively. The optimal pH at 55$^{\circ}C$ and the optimal temperature at pH 7.0 were 8.0 and 60$^{\circ}C$, respectively. The D-values of the enzyme at 60, 65, and 70$^{\circ}C$ were 22, 2.1, and 0.75 hrs, respectively. The enzyme activity was significantly inhibited in the presence of 1 mM o-phenanthroline or EDTA, suggesting that the enzyme is metalloprotease. The $K_m$, and $V_{max}$ for Hammarsten casein were found to be 3.2 mg/ml and 0.918 unit/ml, respectively. These enzymatic properties were similar to those of elastase produced from P. aeruginosa IFO 3455, but the enzyme was clearly different from the reported elastase, in respect to $Ca^{++}$ effects on enzyme-thermostability. This property, together with amino acid composition analysis, confirmed that the enzyme differs from the known P. aeruginosa elastase.

• Journal of Life Science
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• v.12 no.6
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• pp.682-687
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• 2002

We analyzed improvement on the enzyme activity of CPase Taq by addition of various metal ions. The enzyme activity was increased more then four times by 1 mM cobalt ion and almost three times by 1 mM calcium ion. However, the active center metal zinc ion did not affect the enzyme activity. In order to investigate whether the active center metal affects the enzyme activity, zinc ion which is occupied the active center of the enzyme was replaced by cobalt ion which activates the enzyme activity very effectively. Since the cobalt ion in the active center of the cobalt-substituted CPase Taq did not affect the enzyme activity, it could act as the natal metal ion in the active center of the enzyme.

• Preventive Nutrition and Food Science
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• v.11 no.2
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• pp.140-145
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• 2006

Seventy eight bacterial strains were isolated from several jeotgals using MRS and M 17 agar media. The probiotic properties such as tolerance of extreme growth condition, production of antimicrobial compound, production of hydrogen peroxide, and enzymatic activity of bile salt hydrolase were investigated. DHK 4, 10, 21 and 74 strains showed_a strong tolerance property against extreme conditions such as low pH and 0.5% oxgall-supplemented medium. DHK 10 and 47 strains produced hydrogen peroxide on TMB agar plate. DHK 8 and 10 strains produced antimicrobial compounds onto MRS agar against E. facalis. DHK 4, 6, 21, 29, 33, 63 and 87 strains had high activities of bile salt hydrolase. Especially, DHK 10 displayed a strong probiotic candidate; the abilities to produce the antimicrobial compound, hydrogen peroxide, and bile salt hydrolase. All these strains are assumed to be useful probiotic candidates. Among 78, twenty seven strains which have probiotic properties were tentatively identified by 16S rRNA sequencing. Among them, 7 Lactobacillus spp., 6 Leuconosotoc spp., 2 Weisella spp., 1 Pediococcus sp., 1 Staphylococcus sp., 1 Enterococcus sp. and 2 Streptococcus spp. were tentatively identified.

• Food Science and Biotechnology
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• v.18 no.2
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• pp.488-493
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• 2009

A protein isolate was prepared from black soybean (Glycine max L. Merrill) that possessed higher antioxidant activity than ordinary white soy protein isolates. The isolate was partially hydrolyzed by alcalase to reduce the allergenicity of black soybean. Alcalase remarkably reduced the molecular mass of the major soybean allergens that have molecular weights of 53, 38, and 24 kDa. Hydrolytic breakdown occurred more effectively in Gly m Bd 30K than in Gly m Bd 60K or Gly m Bd 28K. Alcalase hydrolysis increased the solubility and hydrophobicity of the black soybean protein isolate. The foaming activity and stability of black soybean proteins were highly increased by the partial hydrolysis.

• Preventive Nutrition and Food Science
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• v.1 no.1
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• pp.111-116
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• 1996

Polyphenol oxidase(PPO) isolated from the crude extract of ascidian, Halocynthia roretzi, showed higher affinity for catechol than tyrosine or DL-DOPA. Successful enzyme assay could be performed at $25^{\circ}C$, 10min. by mixing 0.2ml of crude enzyme extract with 2.8ml of 0.13M catechol in 0.1M sodium phosphate buffer(pH 6.4). The specific activity of PPO which had been purified with a combination of ammonium sulfate treatment, ion exchange chromatography on DEAE-cellulose, and gel filtration on Sepharose 6B was 13-fold disc gel electrophoresis. The activity of PPO was stable from pH 5.0 to 8.0 and showed the peak activity at pH 6.4 .The optimum reaction temperature for PPO oxidation on catechol was 35$^{\circ}C$ and those enzyme were heat stable up to 4$0^{\circ}C$. Molecular weigth of the enzyme was estimated about 170kDa. One molecule was found to be composed of gour subunits. Two of them had molecular weigh of 55kDa and the others 30kDa. The {TEX}$K_{m}${/TEX} values, {TEX}$V_{max}${/TEX} and catalytic efficiency({TEX}$V_{max}${/TEX}/{TEX}$K_{m}${/TEX}) for catechol were 0.12mM, 2.5mM/liter/min. and {TEX}$0.18min^{-1}${/TEX} respectively. The substrate affinity and electrophorectic pattern suggested that the enzyme of ascidian was considered to be not tyosine but catechol oxidase.

• Food Engineering Progress
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• v.15 no.4
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• pp.413-419
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• 2011

For producing a high added-value natural seasoning ingredient, a yeast extract (Yx) was supplemented with a rice protein residue fermented with Bacillus licheniformis (Rfl) or with Bacillus subtilis (Rfs). A rice protein residue was obtained after enzymatic hydrolysis of rice protein which was used for preparing a yeast culture medium. Overall acceptabilities of the supplemented yeast extracts (YxRfl or YxRfs) were higher compared to pure yeast extract. Savory taste like umami was found to increase noticeably by adding a fermented rice protein residue to yeast extract, which was confirmed in taste sensor analysis and in sensory test. Beyond the presence of savory tasting amino acids such as Glu and Asp in a fermented rice protein residue, it is assumed that other soluble peptide fractions remained play an important role in enhancing taste of the supplemented yeast extracts. Thus, the yeast extract added with a fermented rice protein residue could be applied to manufacture a natural seasoning ingredient.

• Food Science of Animal Resources
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• v.41 no.4
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• pp.608-622
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• 2021

Bioactive peptides have great potentials as nutraceutical and pharmaceutical agents that can improve human health. The objectives of this research were to produce functional peptides from ovotransferrin, a major egg white protein, using single enzyme treatments, and to analyze the properties of the hydrolysates produced. Lyophilized ovotransferrin was dissolved in distilled water at 20 mg/mL, treated with protease, elastase, papain, trypsin, or α-chymotrypsin at 1% (w/v) level of substrate, and incubated for 0-24 h at the optimal temperature of each enzyme (protease 55℃, papain 37℃, elastase 25℃, trypsin 37℃, α-chymotrypsin 37℃). The hydrolysates were tested for antioxidant, metal-chelating, and antimicrobial activities. Protease, papain, trypsin, and α-chymotrypsin hydrolyzed ovotransferrin relatively well after 3 h of incubation, but it took 24 h with elastase to reach a similar degree of hydrolysis. The hydrolysates obtained after 3 h of incubation with protease, papain, trypsin, α-chymotrypsin, and after 24 h with elastase were selected as the best products to analyze their functional properties. None of the hydrolysates exhibited antioxidant properties in the oil emulsion nor antimicrobial property at 20 mg/mL concentration. However, ovotransferrin with α-chymotrypsin and with elastase had higher Fe³⁺-chelating activities (1.06±0.88%, 1.25±0.24%) than the native ovotransferrin (0.46±0.60%). Overall, the results indicated that the single-enzyme treatments of ovotransferrin were not effective to produce peptides with antioxidant, antimicrobial, or Fe³⁺-chelating activity. Further research on the effects of enzyme combinations may be needed.