• The Korean Journal of Food And Nutrition
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• v.8 no.3
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• pp.192-198
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• 1995

For the production of EMC, various professes and lipases were used to hydrolyse cheese sulk. The optimal conditions of various proteases were as follows, pronase-3$0^{\circ}C$, p14 7.0, pancreatln-4$0^{\circ}C$, pH 8.0, pacific protease-3$0^{\circ}C$, pH 7.0 and protease from Asp. sp. -5$0^{\circ}C$, pH 8.0. The optimal conditions of various lipases were as follows ; pancreatic lipase-5$0^{\circ}C$, pH 8.0, palatase ML-5$0^{\circ}C$, pH 7.0 and lipase form Candida -4$0^{\circ}C$, pH U.0. After hydrolysation under optimal conditions, the amounts of free amino acid and free fatty ac14 were increased with reaction time. Hydrolysates of pacific protease and pronase were showed high amount of free amino acid(0.67mg/ml and 0.74mg/ml). Especially EMC had high amount of glutamic acid and leucine. Lipase from Candida cylindracea produced high amount of free fatty acid (24.63 mg/ml) Butyric acrid, palmitic acid, stearic acid and oleic acid among free fatty acids were showed high amounts. Sensory evaluation of various MC were tasted nth 8 panelist. EMC produced with pancreatic lipase was most bitterness and EMC produced with palatase ML was best acceptable cheese flavor.

• Korean Journal of Food Science and Technology
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• v.22 no.5
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• pp.590-595
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• 1990

The destructive effect of peroxidized lipid on the amino acid in protein isolate and the proteolytic activity of protease were studied in the model system of rice bran. The content of amino acids in the protein isolate decreased significantly when they reacted with peroxidized lipid (pov. 1200 meq/kg). Most of amino acids were lost by more than 90% in salt soluble protein isolates when analyzed by the method of enzyme hydrolysis. Formaldehyde reduced the activity most severely among peroxidized products. Formic acid, peroxidized lipid and hydroperoxide were also found to reduce the protease activity. The damaging effect of the secondary products on the protease activity was more serious than that of the primary products of lipid peroxidation. The destruction of amino acids in the total protein and Inhibition of protease activity by the peroxidized lipid were apparent.

• Korean Journal of Food Science and Technology
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• v.13 no.3
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• pp.241-246
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• 1981

A fungal strain which produced high levels of acid protease and amylase was isolated from the atmosphere for application to the manufacture of digestive enzme preparation. This study was carried out to elucidate its microbiological characteristics, environmental conditions for production of the enzymes, and relationships between the enzyme activity and acidity. 1. The isolate was identified as a fungal strain which belonged to Aspergillus niger by the manual of Rafer and Fennel, and was found to be a strain producing high levels of acid protease and amylase. 2. The optimal pH of tile enzymes produced by the strain were: protease, 2.0;, ${\alpha}-amylase$, 4 to 5; and glucoamylase, 3 to 5. 3. The optimal culture conditions for production of the enzymes were: protease (at pH 2.5), 2 to 3 days incubation on wheat bran at $30^{\circ}C$; ${\alpha}-amylase$ and glucoamylase(at pH 3.0), 3 days incubation at $30^{\circ}C$. 4. The production of acid protease and glucoamylase was increased approximately by 20 percent when 2 percent of corn starch was added to the wheat bran medium. 5. The addition of 0.3 percent ammonium sulfate to the wheat bran medium resulted in enhancing the enzyme production, especially of acid prctease.

• Korean Journal of Food Science and Technology
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• v.46 no.6
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• pp.702-709
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• 2014

Normal alcoholic fermentation took place at $20-25^{\circ}C$ in yakju (traditional Korean rice wine) prepared without the addition of protease (non-addition group). The total concentration of organic acids increased by 1.0-2.7 fold in the non-addition group. While the concentration of lactic acid and acetic acid increased, the pyroglutamic acid concentration decreased by 51.1 fold. Consequently, the total acidity and volatile acid concentration increased, and the overall pH decreased. Compared to the addition group, the non-addition group showed a 3.0-5.2 fold increase in the amount of amino acids; however, the total estimated concentrations of free-form amino acids were 5.2-11.9 times lower than those in the latter group. The major amino acids found in the non-addition group were alanine, arginine, leucine, and phenylalanine. The yakju preparation from the non-addition group showed a 1.2-3.0 fold decrease in the final color intensity as compared to that from the addition group.

• Korean Journal of Microbiology
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• v.20 no.3
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• pp.105-112
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• 1982

The strain of Aspergillus, 6368A, producing acid protease showing high activity was isolated from soil, as a result of wide research about mold group. This strain was identified as a species of Aspergillus tubingensis by the investigation of morphological characteristics. The change of the enzyme production under the various media and culture condition was also studied. The optimum pH and stability of crude acid protease are 2.5, 2.0~4.5 and the optimum temeprature and thermal inactivation waas shown $50^{\circ}C,\;55^{\circ}C$, respectively. From the result of the study on the effects of metal ions, it was found that $MnCl_2,\;CoCl_2,\;CuCl_2,\;SrCl_2,\;and\;NiCl_2$ slightly increased the enzyme activity, on the other hand $ZnCl_2,\;CaCl_2,\;MgCl_2,\;SLS,\;and\;KMnO_4$ decreased it.

• CELLMED
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• v.4 no.1
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• pp.6.1-6.12
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• 2014

Anthrax is the deadly disease for human being caused by Bacillus anthracis. Instantaneous research work on the mode of infection of the organism revealed that different proteases are involved in different steps of pathogenesis. Present study reports the in silico characterization and the detection of pathogenic proteases involved in anthrax infection through protein-protein interaction. A total of 13 acid, 9 neutral, and 1 alkaline protease of Bacillus anthracis were selected for analysing the physicochemical parameter, the protein superfamily and family search, multiple sequence alignment, phylogenetic tree construction, protein-protein interactions and motif finding. Among the 13 acid proteases, 10 were found as extracellular enzymes that interact with immune inhibitor A (InhA) and help the organism to cross the blood brain barrier during the process of infection. Multiple sequence alignment of above acid proteases revealed the position 368, 489, and 498-contained 100% conserved amino acids which could be used to deactivate the protease. Among the groups analyzed, only acid protease were found to interact with InhA, which indicated that metalloproteases of acid protease group have the capability to develop pathogenesis during B. anthracis infection. Deactivation of conserved amino acid position of germination protease can stop the sporulation and germination of B anthracis cell. The detailed interaction study of neutral and alkaline proteases could also be helpful to design the interaction network for the better understanding of anthrax disease.

• Applied Biological Chemistry
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• v.6
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• pp.107-117
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• 1965

(1) In order to study the specificity of Aspergillus soya protease to soybean protein, as well as the types of peptides formed during soybean-koji prerapation the amino acid sequence for the di & tripeptide and N-terminal amino acid residue and C-terminal amino acid residue were identified. As the results of the study, the following were obtained. Gly, Glu. Ala. Ser. Glu. Ser. Ala. Val (Cys, Glu, Ser, Ala, Arg, Try, Leu or Ileu) Asp. Phe (His, Arg, Cys, Asp, Ser, Ala, Leu or Ileu) Glu. Ala (Cys, Gly, Met) Glu. Ala (Asp, Glu,) Gly. Met (Asp, Glu, Ala, Tyr, Leu or Ileu, Lys,) Gly. Leu or Ileu (His, Asp, Glu, Gly, Ser, Lys, Thr, Phe,) Cys. Gly (Asp, Tyr,) Glu. Pro (Asp, Glu, Ser, Gly, Thr, Ala, Val, Leu or Ileu) Try. Ser (Gly, Glu, Arg, Ala, Met, Leu or Ileu,) Asp. Met (Asp, Glu, Ala, Try, Pro, Leu or Ileu,) His Thr (Ser, Gly, Tyr, Pro, Leu or Ileu,) Glu. Gly (Asp, Ala, Ser, Glu,) Leu or Ileu (2) It has revealed that Aspergillus soya protease has considerably wider range of specificity than that of chymotrypsin, pepsin and trypsin but not mold protease and Aspergillus saitoi protease. It can be said that Asp. soya protease split the bond adjacent to glutamic acid, aspartic acid, glycine, serine, alanine, cystine, tryptophan, histidine preferably acidic amino acid as C-terminal amino acid residue.

• Journal of the Korean Society of Food Science and Nutrition
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• v.13 no.2
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• pp.193-204
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• 1984

The enzymatic properties of the alkaline AL-protease, which had been prepared from the crude zymolyase of Arthrobzoter luteus, was investigated together with its active amino acid residue. Complete inactivaton of the proteolytic activity of AL-protease by either DFP or PMSF was simultaneously accompanied by the loss of its lytic effect on the lysis of yeast cell wall. In the reaction, AL-protease showed the pattern of inactivation to decrease very slowly, as compared to that of chymotrypsin, and that enzyme and DFP were found to react with a molar ratio of 1 : 1. The preparation of AL-protease exhibited no hydrolytic activity in any substrates of polysaccharases, playing a significant role in the lysis of yeast cell wall. The optimum pH and temperature of AL-protease was pH 10.5 and $65^{\circ}C$, respectively. It also showed stability in the pH range from 5 to 11 and at the temperature below $65^{\circ}C$. Through the identification of the amino acid residue in the active site of the $^{32}P$-diisopropylph-osphorylated(DIP) AL-protease modified specifically with $^{32}P$-labeled DFP, AL-protease was found to be a DFP-sensitive which has a mole of active serine residue involved in its proteolytic activity per mole of the enzyme.

• BMB Reports
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• v.37 no.5
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• pp.574-581
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• 2004

The full-length cDNA of the lumbrokinase fraction 6 (F6) protease gene of Lumbricus rubellus was amplified using an mRNA template, sequenced and expressed in E. coli cells. The F6 protease gene consisted of pro- and mature sequences by gene sequence analysis, and the protease was translated and modified into active mature polypeptide by N-terminal amino acid sequence analysis of the F6 protease. The pro-region of F6 protease consisted of the 44 residues from methionine-1 to lysine-44, and the mature polypeptide sequence (239 amino acid residues and one stop codon; 720 bp) started from isoleucine-45 and continued to the terminal residue. F6 protease gene clones having pro-mature sequence and mature sequence produced inclusion bodies in E. coli cells. When inclusion bodies were orally administrated rats, generated thrombus weight in the rat' venous was reduced by approximately 60% versus controls. When the inclusion bodies were solubilized in pepsin and/or trypsin solutions, the solubilized enzymes showed hemolytic activity in vitro. It was concluded the F6 protease has hemolytic activity, and that it is composed of pro- and mature regions.

• Korean Journal of Food Science and Technology
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• v.21 no.1
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• pp.92-99
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• 1989

The soy milk prepared from soy protein concentrate was treated with pretense of various concentrations. Growth and acid production by Lactobacillus acidophilus or L. bulgaricus in soy milk containing partially hydrolyzed protein were investigated. Sensory evaluation of soy yogurt beverages prepared from pretense treated soy milk was also performed. The treatment of soy milk with pretense markedly enhanced acid production by lactic acid bacteria, particularly by L. acidophilus, whereas pH and number of viable cells were not .affected by pretense treatment. Protease treatment of 15 minutes greatly enhanced acid production by lactic acid bacteria, but further treatment up to three hours did not affect the acidity markedly. The sensory evaluation showed that overall acceptability of soy yogurt beverages was slightly improved when soy milk was treated with pretense of 0.1%. The amount of non-protein nitrogen was considerably increased by pretense treatment of 15 minutes and it reached the maximum value by treatment of two hours.