• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.2
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• pp.211-215
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• 2002

Pretense production and its characteristics were investigated for Rhizopus stolonifer, Rhizopus oryzae and Absidia corymbifera which were isolated from Korean traditional meju. The optimum culture conditions of the strains for the production of protease in basic medium [wheat bran : 1% glucose solution=1 : 1 (w/v)] were 3$0^{\circ}C$ and 4 days. The optimum pH and temperature for the enzyme activity of crude enzymes produced by Rhizopus sto-lonifer, Rhizopus oryzae and Absidia corymbifera were pH 6.0 and 5$0^{\circ}C$, respectively. The enzymes were relatively stable at pH 4.0~7.0, at temperature below 4$0^{\circ}C$, and at NaCl concentration lower than 16%. The $K_{m}$ value for Hammastein casein was 3.3$\times$10$^{-4}$ , 0.75$\times$10$^{-4}$ and 1.3$\times$10$^{-4}$ M, and $V_{max}$ value was 17.2$\mu\textrm{g}$/min, 9.4$\mu\textrm{g}$/min and 7.8$\mu\textrm{g}$/min, respectively.y.

• Food Science and Preservation
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• v.13 no.5
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• pp.563-568
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• 2006

The properties of mung bean were investigated depending on hydrolysis condition. The results showed that enzyme treatments (${\alpha}$-amylase and protease each at 0.1% (w/w)) by varying hydrolysis temperature showed better properties than non-pretense treatment (control group). The treatment with 0.08% ${\alpha}$-amylase was best for optimum hydrolysis of mung bean starch The treatment using a mixture of 0.08% (w/w) ${\alpha}$-amylase and 0.12% (w/w) protease was best for optimum hydrolysis of meg bean protein. The effects of Hydrolysis time of mung bean showed that the optimum time was 60 and 90 min and there fore the optimum time was set at 60 min. These result showed that the best hydrolysis conditions of mung bean were the treatment at $60^{\circ}C$ for 60 min using a mixture of 0.08%(w/w) ${\alpha}$-amylase and 0.12% (w/w) pretense, with the sugar level shown at $5.8^{\circ}Brix$, reducing sugar at 2,022.13 mg% and crude protein at 7,666.17 mg%.

• Korean Journal of Food Science and Technology
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• v.37 no.5
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• pp.827-832
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• 2005

Bacillus subtilis JM3 protease from naturally fermented anchovy sauce was partially purified in 40-60% ammonium sulfate fraction. To accelerate fermentation of anchovy sauce, 2 and 4% crude B. subtilis JM3 proteases were added to 6 month-ripened anchovy sauce, and their hydrolysis degrees and amino-nitrogen contents were investigated at different storage times. Low molecular weight (LMW) peptide was purified by ultrafiltration ana gel permeation chromatography from anchovy sauce manufactured with B, subtilis JM3 protease. Anchovy sauces with 2 and 4% proteases increased hydrolysis rate by 27 and 32%, respectively. Amino-nitrogen contents of anchovy sauces fermented with 2 and 4% proteases were twofold higher than that of control. Control showed five peptide peaks on Bio-Rad P2 gel permeation chromatography spectrum, whereas anchovy sauces with 2 and 4% B. subtilis JM3 proteases showed six and seven peaks, respectively. ACE inhibitory activity was highest in peak 6 (43.75%) of anchovy sauce with 2% protease, followed by peak 5 (34.82%) of control. DPPH radical-scavenging effect was higher than 50% in all samples. Cytotoxicity was highest in peak 3 (44.12%) of control, fellowed by peak 5 (42.04%) of anchovy sauce with 4% protease.

• The Korean Journal of Food And Nutrition
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• v.18 no.1
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• pp.11-18
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• 2005

Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.

• Microbiology and Biotechnology Letters
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• v.25 no.6
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• pp.623-629
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• 1997

The studies of isolation and physiological characteristics of mesophilic or thermophilic bacteria from thermophilic oxic process (TOP) treating Chinese restaurant wastes were conducted. Chinese restaurant wastes were consist of moisture; 75.8%, solids; 24.2% and ash; 0.49%. The volatile solid was about 99% of total dry solids. In wastes used in this experiment, there was content of crude protein; 4.47%, crude lipid; 3.56%, free sugar, 0.4% , crude starch; 10.34% and crude fiber 3.14%, respectively. And then it has about 4,970 kcal/kg-dry solid of Chinese restaurant wastes. From TOP treating the chinese restaurant wastes, 37 strains of mesophilic or thermophilic bacteria were primarily isolated using medium used for the isolation and among them 6 strains of thermophilic and 7 strains of mesophilic bacteria were selected by testing the activities of amylase, cellulase, protease and lipase. TB-1, TB-9 as thermophilic bacteria and MB-15-1, 15-2, MB23 as mesophilic bacteria having strong enzyme activity were selected among isolated strains. All selected strains reduced nitrate to nitrite and they utilized glucose, manose, manitol, and maltose as carbon source. From these MB15-2 was identified as Bacillus cereus, TB1, Bacillus licheniformis and TB9; Bacillus schlegelii.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.3
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• pp.466-472
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• 1997

Peptides separated from fish paste washing liquid of an Alaska pollak (Theragria chalcogramma) were purified and characterized. The fish paste washing liquid (supernatant) was separated by centrifugation of fish paste homogenate. The fish paste washing liquid of $0.5\%$ concentration was hydrolyzed for 24 hour at $50^{\circ}C$ by immobilized protease in bioreactor and decomposing liquid of protein having $50\%$ decomposing rate (OPA method) was obtained. The crude peptide fractions were obtained from this liquid by Dowex 50w $(H^+)$ column chromatograpy. Purified peptides (SP-fraction peptides) were fractionated by using SP-Sepadex C-25 $(H^+)$ column chromatography. Molecular weights and amino acid compositions of these peptides were estimated by Sephadex G-50 column chromatography and HPLC, respectively. when the washed peptides was eluated with $0.6\~0.9\%\;and\;1.2\~2.0\%$ of NaCl, peptides composed of weakly basic amino acids and strongly basic amino acid were respectively eluted. Molecular weights of each peptide fractions showed the broad distribution from 1,000 Da to 3,000 Da in the order of SP-4>SP-3>SP-2>SP-1. Peptides contained a large quantity of glycine, arginine, glutamic acid, and alanine in the washed peptide and its SP-tractions, respectively.

• Parasites, Hosts and Diseases
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• v.52 no.1
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• pp.41-46
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• 2014

The mature domain of a cysteine protease of Spirometra erinacei plerocercoid larva (i.e., sparganum) was expressed in Escherichia coli, and its value as an antigen for the serodiagnosis of sparganosis was investigated. The recombinant protein (rSepCp-1) has the molecular weight of 23.4 kDa, and strongly reacted with the sparganum positive human or mice sera but not with negative sera by immunoblotting. ELISA with rSepCp-1 protein or sparganum crude antigen (SeC) was evaluated for the serodiagnosis of sparganosis using patient's sera. The sensitivity and specificity of ELISA using rSepCp-1 protein were 95.0% (19/20) and 99.1% (111/112), respectively. In contrast, the sensitivity and specificity of ELISA with SeC were 100% (20/20) and 96.4% (108/112), respectively. Moreover, in experimentally infected mice, the sensitivity and specificity of both ELISA assays were 100% for the detection of anti-sparganum IgG. It is suggested that the rSepCp-1 protein-based ELISA could provide a highly sensitive and specific assay for the diagnosis of sparganosis.

• Korean Journal of Food Science and Technology
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• v.2 no.2
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• pp.38-42
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• 1970

The crude enzyme, tamylase, was produced by cultivating the Bacillus subtilis on wheat bran. It is composed of amylase and protease, and can be used as an additive material to the synthetic detergent, Suny which is manufactured by Ae-kyung Oil and Fat Co. Amylase activity of the enzyme as an additive material to the synthetic detergent; 1. is decreased by increasing the amount of detergent. But inhibitory rate under the practical used concentration of detergent is less than ten percents. 2. have optimal temperature at $ 40^{\circ}C$. 3. have optimal pH of substrate on pH $5{\sim}6.5$. 4. is inhibited by $Fe^{+++}$. When enzyme and detergent are mixed both as powder, the enzyme is good for storage. Proteolytic activity is good at the practical used concentration of the detergent, but it is inhibited by strong concentration.

• Korean Journal of Food Science and Technology
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• v.9 no.1
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• pp.31-35
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• 1977

As a study on the acid protease production by Rhizopus japonicus S-62, the culture conditions for the enzyme production and characteristics of the crude enzyme were investigated. The results are summarized as follows: 1. The optimum conditions for solid culture on wheat bran were 48 hrs of culture period and $100{\sim}120%$ addition of tap water. 2. Of the several media, wheat bran medium was the most excellent in the enzyme production. 3. The addition of sucrose, fructose, $NH_4Cl$ and $NaH_2PO_4$ on wheat bran, respectively, increased largely the enzyme production. 4. The optimum pH for the enzyme action was pH $2.4{\sim}2.6$, the optimum temperature was about $40^{\circ}C$, and the stable pH range was $pH\;2.5{\sim}5.0$, the enzyme was stable below $40^{\circ}C$ and was inactivated abruptly above $40^{\circ}C$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.9
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• pp.1273-1279
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• 2006

The quality properties of oak mushroom were investigated using extraction conditions and enzyme treatments. The physiochemical properties were excellent at the extraction temperatures of $20^{\circ}C\;and\;40^{\circ}C$. The quality was increased as the extraction time increased but was best at the extraction time of 10 hr. The physiochemical properties such as soluble solid, reducing sugar and crude protein contents were best at the solvent ratio of 1:100 (w/v) so that it was set at 1:100. Thus, enzyme treatment was done at $50^{\circ}C$ for 2 hr with the solvent ratio of 1:100. The result showed that the best quality was shown using 0.2% protease and 0.2% cellulase. With the enzyme treatment, the essential amino acid contents increased by two folds but no difference was shown in $\beta-glucan$ content.