• 한국동물학회:학술대회논문집
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• 한국동물학회 1994년도 한국생물과학협회 학술발표대회
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• pp.216.2-216
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• 1994

• 한국미생물생명공학회소식지:생물산업
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• 제13권1호
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• pp.28-35
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• 2000

• 한국의류학회지
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• 제37권7호
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• pp.962-971
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• 2013

We compared the effectiveness of amidase (amano acylase, AA) and an endopeptidase, (trypsin, TR) in modifying the hydrophobicity of polyamide fabric. We evaluated the number of amino groups released into the reaction mixture in order to optimize the treatment conditions. We found that a large number of amino groups were released into the reaction mixture due to the cleavage of amide bonds by AA hydrolysis; however, the TR hydrolysis exhibited a relatively lower activity compared to AA hydrolysis. In AA and TR hydrolysis, significant differences were observed in the K/S values and moisture regain. Amide bonds in polyamide fabric were hydrolyzed by AA hydrolysis effectively. Compared to TR, AA formed more hydrolysis product (amino groups) on the fabric surface. Thus, the hydrophobicity of polyamide fabric was modified using AA hydrolysis (as verified by the wettability test) without any deterioration of fiber strength.

• 대한약학회:학술대회논문집
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• 대한약학회 2002년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2
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• pp.331.3-332
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• 2002

A novel penicillin G acylase (PGA)-producing bacterial strain was isolated from soil by using the Serratia marcescens overlay technique. The isolated strain was identified as Leclercia adecarboxylata based on the analyses of the biochemical characteristics (API 20E). the cellular fatty acid profile. and the 16S rDNA sequences. The gene encoding the PGA (pac gene) was cloned into the pHSG399 vector and the recombinant E. coliHB101 clones harboring the pac gene were isolated on agar plates containing phenylacetyl-L -leucine and penicillin G. (omitted)

• Journal of Microbiology and Biotechnology
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• 제29권6호
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• pp.913-922
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• 2019

Magnetic $Ni_{0.7}Co_{0.3}Fe_2O_4$ nanoparticles that were prepared via the rapid combustion process were functionalized and modified to obtain magnetic $Ni_{0.7}Co_{0.3}Fe_2O_4@SiO_2-CHO$ nanocomposites, on which penicillin G acylase (PGA) was covalently immobilized. Selections of immobilization concentration and time of fixation were explored. Catalytic performance of immobilized PGA was characterized. The free PGA had greatest activity at pH 8.0 and $45^{\circ}C$ while immobilized PGA's activities peaked at pH 7.5 and $45^{\circ}C$. Immobilized PGA had better thermal stability than free PGA at the range of $30-50^{\circ}C$ for different time intervals. The activity of free PGA would be 0 and that of immobilized PGA still retained some activities at $60^{\circ}C$ after 2 h. $V_{max}$ and $K_m$ of immobilized PGA were 1.55 mol/min and 0.15 mol/l, respectively. Free PGA's $V_{max}$ and $K_m$ separately were 0.74 mol/min and 0.028 mol/l. Immobilized PGA displayed more than 50% activity after 10 successive cycles. We concluded that immobilized PGA with magnetic $Ni_{0.7}Co_{0.3}Fe_2O_4@SiO_2-CHO$ nanocomposites could become a novel example for the immobilization of other amidohydrolases.

• 약학회지
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• 제27권3호
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• pp.185-205
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• 1983

Penicillins and cephalosporins are biosynthesized from L-.alpha.-aminoadipic acid, L-cysteine and L-valine. A tripeptide, LLD-$\delta$-($\alpha$-aminoadipyl)cysteinylvaline(LLD-ACV) was isolated from fermentation broths of Cephalosporium acremonium as well as of Penicillium chrysogenum and it was proved that the LL-$\delta$-($\alpha$-aminoadipyl cysteine was formed first in mycelia, to which valine would be connected to give LLD-ACV. However, several points are still unsolved; first, what mechanism is involved in the configurational change from L-valine to D-valine, second, what kind of cyclization mechanism gives a $\betha$-lactam ring and a thiazolidine ring and third, what is the pathways for the ring expansion from penicillins to cephalosporins. At present, it seems clear that LLD-ACV is cyclized to give isopenicillin N, which is transformed to penicillin N and further to cepbalosporin C. Other hydrophobic penicillins, including benzyl penicillin and penicillin V, are formed from isopenicillin N by acyl-exchange reactions catalyzed by penicillin transferase, rather than by acylation reaction on 6-aminopenicillanic acid(6-APA), which was isolated from the fermentation broth of P. chrysogenum and which would be formed by hydrolysis of $\delta-(\alpha$-amincadipyl)amido moiety at the C-6 position in isopenicillin N or penicillin N by penicillin acylase. Acylation of 6-APA is catalyzed also by penicillin acylase, but the reaction is proved not to be involved in penicillin biosynthesis. Understanding the biosynthesis of penicillins and cephalsoporins would provide solutions to increase in fermentation yields of penicillins, especially of cephalosporins and a solution to biological production of 7-aminocepbalosporanic acid (7-ACA) which is of importance in pharmaceutical industry. Still regulation mechanisms in penicillin and cephalosporin biosynthesis are unveiled at all.

• 한국미생물·생명공학회지
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• 제23권5호
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• pp.556-558
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• 1995

A strain which showed cephalosporin C resistance and 7-aminocephalosporanic acid sensitivity was isolated from nature. Among the isolates, SS5 was sensitive to cephalosporin C, penicillin G, ampicillin, 7-aminocephalosporanic acid, 6-aminopenicillanic acid, and 7-aminodeacetoxy cephatosporanic acid at concentrations of 1,000 $\mu $g/ml, 2,000 $\mu $g/ml, 3,000 $\mu $g/ml, 30 $\mu $g/ml 100 $\mu $g/ml and 100 $\mu $g/ml, respectively. But SS5 was sensitive at very low concentration of chloramphenicol, kanamycin, neomycin, streptomycin and tetracycline. Since SS5 was sensitive to 7-ACA (30 $\mu $g/ml) and didn't have $\beta $-lactamase activity on the cephalosporin C, SS5 could be useful as an indicator strain for the production of 7-ACA, which is an important precursor for the synthesis of many semisynthetic cephalosporins.

• Journal of Microbiology
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• 제43권spc1호
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• pp.101-109
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• 2005

To gain maximal benefit in a competitive environment, single-celled bacteria have adopted a community genetic regulatory mechanism, known as quorum sensing (QS). Many bacteria use QS signaling systems to synchronize target gene expression and coordinate biological activities among a local population. N-acylhomoserine lactones (AHLs) are one family of the well-characterized QS signals in Gram-negative bacteria, which regulate a range of important biological functions, including virulence and biofilm formation. Several groups of AHL-degradation enzymes have recently been identified in a range of living organisms, including bacteria and eukaryotes. Expression of these enzymes in AHL-dependent pathogens and transgenic plants efficiently quenches the microbial QS signaling and blocks pathogenic infections. Discovery of these novel quorum quenching enzymes has not only provided a promising means to control bacterial infections, but also presents new challenges to investigate their roles in host organisms and their potential impacts on ecosystems.

• 한국미생물·생명공학회지
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• 제40권2호
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• pp.83-91
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• 2012

본 총설은 N-acyl-homoserine lactone (AHL)에 기반한 quorum sensing(QS)을 비롯한 다양한 QS 시스템 및 생물막 형성과의 관련성에 대한 연구 동향을 정리하였다. 또한 anti-QS으로서 quorum quenching 전략을 이용한 생물막 억제 연구 동향에 대해 중점적으로 서술하였다. 세균의 독특한 신호전달 체계인 QS는 AHL과 같은 특정한 신호분자의 농도에 의해 세균의 집단적 행동 양식이 결정되는 세포밀도-의존성 유전자 발현 조절 메커니즘이다. QS 시스템은 미생물의 부착 및 생물막 형성에 있어 중요한 역할을 한다. AI-1이나 AI-2에 의한 QS는 생물막 형성 과정에 필요한 세포외 다당류, 단백질, 세포 외 DNA 등 주요한 구성 성분 등의 생산뿐만 아니라, 세균의 운동성 조절, 부착, 생물막 해체 과정까지도 조절하는 기능을 한다. 일부 세균의 경우 QS시스템 이외에도 second messenger로 알려진 c-di-GMP에 의한 signaling이 QS와 서로 연결되어 생물막 형성이나 병독성과 같은 타깃들을 함께 조절한다. 생물막은 병원성 세균에 의한 감염 시 여러 가지 병독성 가운데 가장 중요한 요소 중 하나이기 때문에, 생물막 형성을 조절하는 QS를 차단하기 위한 다양한 anti-quorum sensing 전략이 연구되고 있다. Anti-QS 접근 방식은 의학적 이용뿐만 아니라 물에 노출되어있는 MBR을 비롯한 많은 산업적 장치 등에서 생물막 형성으로 인한 손상 및 오염을 방지하기 위해 쓰일 수 있다. Anti-QS 전략 중 신호분자인 AHL을 무력화 시키는 quorum quenching 효소(AHL-lactonase, AHL-acylase, oxidoreductas)를 이용하여 생물막 형성을 억제할 수 있으며, 막을 이용한 수처리 공정에서 막에 발생하는 biofouling을 완화시킬 수 있는 새로운 anti-fouling 처리 기술로서 이러한 QQ 효소의적용 가능성을 보여 주고 있다.

• Journal of Microbiology and Biotechnology
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• 제11권2호
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• pp.199-203
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• 2001

A simple quantitative method to measure the degree of silanization was developed, based on the reaction of ninhydrin with the silanization reagent (3-aminopropyltriethoxysilane, 3-APTES). At low concentrations (0.001-0.005%, v/v) of 3-APTES, a good linearity was obtained when 3-APTES reacted with undiluted ninhydrin for 30 min. On the other hand, at high levels of 3-APTES, a linearity was obtained when 3-APTES reacted with 3-fold diluted ninhydrin for 20 min. The reliability of regression curves mentioned above was expressed as a regression coefficient ($R^2$) of more than 0.99. Immobilization of different enzymes was introduced via silanization by using the 3-APTES in order to confirm the validity of the ninhydrin method. When yield for each step in the immobilizatio process were compared, yields of both glutaraldehyde and protein were founc to have the same tendency to silanization. These results shw that the ninhydrin method was suitable for quatitative analysis of silanization and that yields of immobilization could be pre-estimated by measuring silanization levels using the ninhydrin method.