• Title/Summary/Keyword: protease production

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Multiple Chromosomal Integration of a Bacillus Ya-B Alkaline Elastase Gene (고초균(Bacillus) 염색체상에서 외래 유전자 Alkaline Elastase Gene의 증폭)

  • 김병문;정봉현
    • Microbiology and Biotechnology Letters
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    • v.23 no.5
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    • pp.544-549
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    • 1995
  • The alkaline elastase is an extracellular serine protease of the alkalophilic Bacillus strain Ya-B. To increase the gene copy number and the production level of the alkaline elastase Ya-B, we designed, on the B. subtilis chromosome, a gene amplification of the 10.6 kb repeating unit containing amyE, aleE (alkaline elastase Ya-B gene) and tmrB. The aleE was inserted between amyE and tmrB, and B. subtilis APT119 strain was transformed with this amyE-aleE-tmrB-junction region fragment. As a result, we succeeded in obtaining tunicamycin-resistant (Tm$^{r}$) transformants (Tf-1, Tf-2) in which the designed gene amplification of 10.6 kb occurred in chromosome. The transformants showed high productivity of $\alpha $-amylase and alkaline elastase Ya-B. The copy number of the repeating unit (amyE-aleE-tmrB) was estimated to be 25, but plasmid vector (pUC19) was not integrated. The amplified aleE of chromosome was more stable than that of plasmid in absence of antibiotics.

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Isolation of Pseudomonas aeruginosa 90-2-2205 Producing the S-type Pyocin from Korean Patients and the Pyocin Production (한국환자유래의 S형 Pyocin 생성균주 Pseudomonas aeruginosa 90-2-2205의 분리 및 Pyocin 생산)

  • 김란숙;이정미;김병오;박영덕;진익렬
    • Microbiology and Biotechnology Letters
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    • v.21 no.2
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    • pp.125-131
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    • 1993
  • The s-type pyocin, one kind of bacteriocins, is a bactericidal substabce of protein nature produced by certain Pseudomonas aeruginosa and is active against some other strains of the same or closely related species. Among many Pseudomonas aeruginosa strains collected from the patients at the Hospitals in Seoul and Taegu cities, some Pseudomonas aeruginosa pyocinogeny were determined by pyocin typing. As a result, Pseudomonas aeruginosa 90-2-2205 was selected as the S-type pyocin producing microorganism due to its highest antimicrobial and protease sensitivity.

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Role of dendritic cells in infectious disease and tumor (감염질환(infectious disease)과 종양면역(tumor immunity)에 있어서 수지상 돌기세포(dendritic cells)의 역할)

  • 임종석;김광동
    • The Microorganisms and Industry
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    • v.26 no.1
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    • pp.8-17
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    • 2000
  • Thirtythree strains of the Aspergillus spp. isolated from foodstuffs were observed through some physiological characteristics for detection of identification key of Aspergillus spp. 1) Each strain of Aspergillus spp. had their specific characteristics and could be used for identification of species. 2) Excellent amylase-producing fungi were observed among the isolated strains of Aspergillus spp. 3) Amylase activities increased for one week incubation period. 4) In the tests of common characters of aflatoxin-producing fungi among the 33 strains of Aspergillus spp., for example, conidial size, presence of sclerotia, kojic acid, and pigment production, coloration of phenol, reduction of methylene blue, etc.

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Isolation and identification of Bacillus sp, GS Producing Xylanase (Xylanase생산성 Bacillus sp. GS의 분리 및 동정)

  • An, Jun-Bae;Park, Heon-Guk;Lee, Gye-Ho
    • The Korean Journal of Food And Nutrition
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    • v.7 no.1
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    • pp.8-15
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    • 1994
  • To utilize hemicellulosic biomass efficiently, the microorganism producing xylanase was isolated from fermented sawdust. It was a Gram positive, aerobic and rod shape bacterium. It had endospore and secreted strong hydrolases, such as amylase and protease. Through morphological, cultural and physiological tests, it was identified as Bacillus sp. GS. To increase the productivity of xylanase from Bacillus sp. GS, the enzyme production medium was optimized. The composition of the medium and incubation conditions were like follows xylan 1.25%, yeast extract 0.1%, NaN030.2%, K2HP04 0.1%, MgSO4 0.02%, mineral salt 0.005%, pH 6.5, incubation temperature 37$^{\circ}C$.

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Evaluation of the Ripening Degree and Functional Properties on Enzyme Modified cheese (Enzyme Modified Cheese의 숙성도 및 기능성 평가)

  • Seo, Hyeong-Ju;Hong, Jae-Hun;Son, Jong-Yeon
    • The Korean Journal of Food And Nutrition
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    • v.9 no.2
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    • pp.143-150
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    • 1996
  • The studies was carried out to investigate ripening degree and functional properties of EMC produced with pancreatic protease and palatase ML. During production of EMC, the amounts of free amino acid and free fatty acid were increased with increasing the reaction time. The amount of total nitrogen(T-N) and water soluble nitrogen(WSN) were increased with increasing time. EMC had contents of 1.79eA T-N and 0.52o WSN at 60 min of hydrolysis time. SRI and FRI value had also a similar correlationship. On the gel filtration, 2 kinds of soluble proteining capacity was also shown in alkali solution. Furthermore the foaming stability had the same result as that of the solubility. The water absorption of EMC showed the highest level at pH 4.0 and 5.0.

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Extracellular Proteinase를 생산하는 효모의 분리동정과 효소의 생산

  • Kim, Chnag-Hwa;Lee, Tae-Hyung;Yu, Choon-Bal;Jin, Ingnyol
    • Microbiology and Biotechnology Letters
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    • v.24 no.4
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    • pp.452-458
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    • 1996
  • A yeast strain TH65 producing a high level of proteinase under alkaline condition was isolated, and identified as Yarrowia lipolytica by morphological, physiological, and biochemical characteristics. In proteinase productivity, glycerol and glucose among tested carbon sources were very effective, and optimum concentration of glucose was 0.5%. Skim milk was found to be most effective nitrogen source in productivity, and its optimum concentration was 0.6%. But, cysteine, cystine and tryptophane decreased the proteinase productivity. Yeast extract was relatively effective at the range of 0.1-0.5%. The yeast showed maximum production of proteinase at 18$\circ$C, pH 9-11, and cultivation time of 36 hours.

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Partial Characterization of an Anti-Listerial Bacteriocin from Enterococcus faecium CJNU 2524

  • Yang, Jung-Mo;Moon, Gi-Seong
    • Food Science of Animal Resources
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    • v.41 no.1
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    • pp.164-171
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    • 2021
  • Listeria monocytogenes is a representative foodborne pathogen and causes listeriosis. Enterococcus faecium CJNU 2524 was confirmed to produce a bacteriocin with anti-listerial activity. To establish optimal culture conditions for the production of the bacteriocin from E. faecium CJNU 2524, different media (MRS and BHI broth) and temperatures (25℃, 30℃, and 37℃) were investigated. The results showed that the optimal culture conditions were MRS broth and 25℃ or 30℃ temperatures. The crude bacteriocin was stable in a broad range of pH conditions (2.0-10.0), temperatures (60℃-100℃), and organic solvents (methanol, ethanol, acetone, acetonitrile, and chloroform). The bacteriocin activity was abolished when treated with protease but not α-amylase or lipase, indicating the proteinaceous nature of the bacteriocin. Finally, the bacteriocin showed a bactericidal mode of action against L. monocytogenes. Therefore, it can be a biopreservative candidate for controlling L. monocytogenes in dairy and meat products.

Role of the prophenoloxidase-activating system in the innate immune response and cuticular melanization in the silkworm

  • Kwang Sik, Lee
    • International Journal of Industrial Entomology and Biomaterials
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    • v.45 no.2
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    • pp.43-48
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    • 2022
  • Bombyx mori is a representative industrial insect and is used in silk production. Additionally, it serves as an insect model in molecular studies. To date, various molecular studies on its physiological characteristics, including the innate immune response and cuticular melanization, have been conducted. The melanization, including cuticular melanization, in insects is controlled by the prophenoloxidase-activating system, which is also involved in their innate immune response. In this review, to better understand the molecular mechanisms underlying the prophenoloxidase-activating system in the silkworm, the roles of five biomolecules, namely tyrosine hydroxylase, prophenoloxidase-activating enzyme, phenoloxidase, serine protease homolog, and immulectin, are discussed.

H-1, C-13, and N-15 resonance assignments of ENOD40B, a plant peptide hormone

  • Young Kee Chae
    • Journal of the Korean Magnetic Resonance Society
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    • v.27 no.2
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    • pp.5-9
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    • 2023
  • t ENOD40B, a plant peptide hormone, was doubly labeled with C-13 and N-15 by recombinant production in Escherichia coli. The peptide was prepared by affinity chromatography followed by protease cleavage and reverse-phase chromatography. To elucidate the mode of action against its receptor, sucrose synthase, we proceeded to assign the backbone and side-chain resonances using a set of double and triple resonance experiments. This result will be used to determine the three-dimensional structure of the peptide at its bound state as well as to observe the chemical shift changes upon binding.

Studies on the Enzyme of Rhizopus oryzae - Part I. Production of Acid Protease and Enzymatic Characteristics - (Rhizopus oryzae의 효소(酵素)에 관(關)한 연구(硏究) - 제(第)1보(報), 산성(酸性) Protease 생산(生産) 및 효소(酵素)의 특성(特性) -)

  • Hou, Won-Nyong;Chung, Man-Jae
    • Applied Biological Chemistry
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    • v.22 no.3
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    • pp.135-141
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    • 1979
  • These experiments were conducted to investigate the conditions of the acid protease production by Rhizopus oryzae and the characteristics of crude enzyme. The results obtained were as follows: 1. The optimum culture time and the optimum amount of added water to the wheat bran medium were about 48 hrs and $80{\sim}120%$, respectively. 2. The addition of $(NH_4)_6Mo_7O_{24},\;(NH_4)_2SO_4,\;NH_4NO_3$, casein, and albumin, respectively, as nitrogen sources to the wheat bran medium was effective. Of these, the optimum concentrations of addition of $(NH_4)_6Mo_7O_{24}$ and casein which were the most effective were 0.1% and 1.0%, respectively. 3. The addition of glucose, galactose, maltose, lactose, and soluble starch, respectively, as carbon sources to the wheat bran medium was effective. Of these, the optimum concentration of addition of glucose which was the most effective was 3.0%. 4. The addition of $KH_2PO_4$ as a phosphate salt to the wheat bran medium was effective. The optimum concentration of addition of $KH_2PO_4$ was 0.3%. 5. The optimum pH for the enzyme action was 2.4, the optimum temperature about $40^{\circ}C$, and the stable pH range $2.0{\sim}5.0$. The enzyme was stab1e below $40^{\circ}C$. 6. The enzyme activity increased rapidly for 10 minutes after addition, thereafter it increased slowly. 7. The enzyme activity increased rapidly to 2 ml of addition, but nearly did not increase at the amounts greater than 2ml.

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