• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.597-600
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• 2000

In this study the enzymatic synthesis of ester-linked conjugates of amino acid and monosaccharide in pyridine was tested by the catalysis of Optimase M-440, an alkaline serine pretense. Optimase M-440 showed the higher activity in the reaction of monosaccharides which have one or more primary -OH groups. And also Optimase M-440 showed high regioselectivity; The transesterification of primary -OH group selectively occurred.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2000.10a
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• pp.117-118
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• 2000

매년 많은 식중독 사고가 보고되고 있는데, 특히 우리나라에서는 생선의 소비량이 많기 때문에 Salmonella 다음으로 Vibrio에 의한 식중독 사고가 높은 것으로 보고되고 있다. 이러한 세균성 식중독은 일반적으로 미생물이 숙주세포에 침입을 해야 하는데, 이를 위해 우선적으로 숙주세포 표면의 여러 단백질 층을 분해해야 한다. 이때 작용하는 단백질 분해효소가 병원성에 직ㆍ간접적으로 관여된다고 생각되고 있으며, 비브리오균이 생산하는 여러 가지 단백질 분해효소가 인간이나 어류의 병원성에 관여되어진다고 보고되고 있다. (중략)

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.290-296
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• 1998

Interspecific hybrids between Aspergillus oryzae var. oryzae and Penicillium chrysogenum (Tyr$\^$-/), high alkaline protease producing fungi, were obtained by nuclear transfer technique. Nuclei isolated from the wild type Aspergillus oryzae var. oryzae strain were transferred into auxotrophic Penicillium chrysogenum mutants and selected the new strains showing an increased protein degrading capability. Maximum production of protoplasts were obtained by 1% Novozym 234 at $30^{\circ}C$ for 3 hours and the most effective osmotic stabilizers for the isolation of protoplasts were 0.6M KCl. Frequencies of hybrid formation by nuclear transfer were 1.3${\times}$10$\^$-3/∼2.8${\times}$10$\^$-3/. They could be suggested as an aneuploid by the observation of genetic stability, conidial size, DNA content, and nuclear strain. The hybrids showed 1.1～2.2 fold higher alkaline pretense activities than parental strains.

• Journal of environmental and Sanitary engineering
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• v.9 no.1
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• pp.89-96
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• 1994

This report was investigate the biological characteristic of $\delta$-endotoxin of product by TH109 strain, one strain TH109 which has toxicity on Cockroach is isolate and identification. Generally the $\delta$-endotoxin of product by 3. thuringiensis strain was easily soluble in acid, alkaline and organic solvents but $\delta$-endotoxin of product by TH109 strain are insoluble in HCI, NaOH Thiol- reagent(25mM Dithiotheritol, 25mM Dithioeryritol, 25mM Nathioglycolate, 0.2M ESCN, 2% v/v $\beta$-mecaptethanol), organic solvents( acetone, $CCI_{4}$, ether, dioxin MeOH chloroforrh xylene ), Protease. Through this study of $\delta$-endotoxin produced by TH109 strain is insoluble in acid, alkaline, organic solvents and pretense etc. In the point of view, it is greater possibility that $\delta$-endotoxin will be transform into toxin by the reducible materials instead of the reaction of protease in the intestine.

• Journal of the Korean Society of Food Science and Nutrition
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• v.6 no.1
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• pp.27-33
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• 1977

The alkaline protease was isolated from the culture of Penicillium species (P-46) grown in the wheat bran media. The crude purification of this enzyme was carried out by extraction with distilled water and precipitated with 0.7-saturated ammonium sulfate, then dialysis for 3days. The activity of this enzyme was determined by Folin's colorimetric method. The results were as follows; 1. The optimum pH and temperature of this enzyme were pH 8.4 and $45^{\circ}C$. 2. This enzyme was stable at pH $7.0{\sim}9.0$. 3. This enzyme was not inactivated by treatment in lower temperature than $30^{\circ}C$. 4. The activity of this enzyme was strongly inhibited by $Hg^{++}$ and $Cu^{++}$, but slightly by $Ag^+$ 5. This enzyme was not inhibited by cystein, thiourea, ${\varepsilon}-aminocaproic$ acid, 2, 4-DNP, EDTA but strongly inhibited by PCMB.

• Journal of Radiation Protection and Research
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• v.18 no.2
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• pp.61-69
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• 1993

We examined various enzyme activity changes by intraperitoneal injection uranium in the carp liver. These enzyme activity changes can be used as biochemical indicators of internal exposure to uranium. The results were followings ; 1) Total protein concentration decreased by intraperitoneal injection in the carp liver. 2) Lysosomal acid pretense and ${\beta}-glucuronidase$ activities increased in the liver until sixth intraperitoneal injection of uranium, but Lysosomal acid phosphatase activities decreased in the liver until the sixth injection of uranium. 3) Alkaline phosphatase activities sharply increased and Glutamate oxaloacetate Transaminase activities steadily decreased in the liver until the sixth injection of uranium. 4) Creatine %kinase activities steadily decreased and malate dehydrogenase activities sharply decreased in the liver after the primary injection of uranium. Any malate dehydrogenase activities was not detected after sixth injection of uranium.

• Journal of Microbiology
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• v.39 no.2
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• pp.95-101
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• 2001

In an effort to develop an efficient expression and secretion system for heterologous proteins in Aspergilius nidulans, the PCR-amplified coding sequence for alkaline pretense (AlpA) of A. oryzae was cloned into a fungal expression vector downstream of A. nidulans aicA (alcohol dehydrogenase) promoter to yield pRAAlp. Transformation of A. nidulans with pRAAlp gave stable transformants harboring various copy numbers (3 to 10) of integrated alpA gene, from among which 6 representatives were selected. On a medium containing 0.8% ammonium sulfate that represses the expression of the host's own pretense, the alcA prumoter-controlled AlpA expression was strongly induced by threonine but repressed by glucose. The level of AlpA secretion was highest (approximately 666 mU/ml) in transformant ALP6 containing the largest copy number integrated alpA. However, the level of AlpA secretion was not necessarily proportional to the copy numbers of the integrated alpA genes. The N-terminal sequence or the secreted mature AlpA was determined to be Gly-Leu-Thr-Thr-Gln-Lys-Ser and its molecular mass to be approximately 34 kDa, indicating that AlpA is properly processed by the removal of 121 N-terminal amino acids.

• Microbiology and Biotechnology Letters
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• v.16 no.6
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• pp.526-531
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• 1988

Procedure for the purification of pretense from culture broth of Streptomyces sp. SMF301 was developed. It was evident that the strain produced two different proteases of which molecular weights were estimated to be 23, 500 and 38, 900 dalton. It was found that the optimum pH of the smaller was 9.0 and that of the larger was 1.0. The optimal temperature of the alkaline pretense was 5$0^{\circ}C$ and that of the neutral pretense was much more stable than neutral protease at extreme condition viz. high temperature, and pH.

• Applied Biological Chemistry
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• v.49 no.4
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• pp.304-308
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• 2006

To extract insoluble proteins from silkworm pupa meal, the meal was treated with pretense produced by Bacillus sp. JH-209. The extraction of insoluble silkworm pupa protein was enhanced at alkaline pHs ranged from 7 to 11 by treatment with the protease. The optimum extraction temperature was $40^{\circ}C$ for in soluble protein treated with pretense. The optimum protease treatment time for extraction of protein was 11 hrs and optimum amount of enzyme treated for extraction of protein was 60 Unit, respectively. The treatment of enzyme extracted more protein than ordinary extraction method without pretense. The foaming capacity, foaming stability, emulsion capacity, and emulsion stability of silkworm pupa meal protein extracted by the treatment of the enzymes increased at all pH ranges. Further more oil absorption as well as water absorption capacities of the protein extracted by the treatment of the enzymes were also increased.

• Korean Journal of Microbiology
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• v.41 no.1
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• pp.87-92
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• 2005

Pronase, a protease produced for commercial purpose by Streptomyces griseus, was composed of serine protease, alkaline protease, aminopeptidase and carboxypeptidase complex, and it has been widely used as anti-inflammatory drugs for human therapy. In this study, we developed a new integration vector, pHJ101 derived from pSET152, containing strong promoter, ermE, to overexpress a certain protease gene. Specific PCR primers for cloning of sprA (a gene for S. griseus protease A) and sprB (a gene for S. griseus protease B) genes were designed from the basis of nucleotide sequence in databases and amplified by PCR. Plasmid pHJ201 and pHJ202 were constructed by inserting of amplified each gene in a vector pHJ101. S. griseus HA and S. griseus HB were respectively obtained by conjugal process of a parent strain, S. griseus IFO 13350 with the recombinant Escherichia coli harboring plasmid pHJ201 or pHJ202. When protease activity was measured in flask cultivation, produced protease levels of S. griseus HA and S. griseus HB increased about 5.3 times and 5 times, respectively, more than that of parent strain. And, the constructed integrating plasmid pHJ101 was applicable for overexpression of a certain gene in Streptomyces sp.