KR100834708B1 - Amylase gene isolated from Tricholoma matsutake and protein encoded thereby - Google Patents

Amylase gene isolated from Tricholoma matsutake and protein encoded thereby Download PDF

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KR100834708B1
KR100834708B1 KR1020070010691A KR20070010691A KR100834708B1 KR 100834708 B1 KR100834708 B1 KR 100834708B1 KR 1020070010691 A KR1020070010691 A KR 1020070010691A KR 20070010691 A KR20070010691 A KR 20070010691A KR 100834708 B1 KR100834708 B1 KR 100834708B1
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amylase
gene
glucoamylase
isolated
genes
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김종국
이진형
김정민
이상한
신기선
김남순
이진만
이은진
신용규
임순옥
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경북대학교 산학협력단
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/52—Genes encoding for enzymes or proenzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2414—Alpha-amylase (3.2.1.1.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405—Glucanases
    • C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
    • C12N9/2411—Amylases
    • C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01001—Alpha-amylase (3.2.1.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
    • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
    • C12Y302/01003—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase

Abstract

An amylase gene isolated from Tricholoma matsutake and a protein expressing the same gene are provided to be applicable as a material for a food industry, a cosmetic industry and a medical industry. An amylase gene is described as SEQ ID : NO. 1 or 2, wherein the amylase is alpha-amylase or gluco-amylase and the gene is isolated from Tricholoma matsutake including useful tradition filamentous fungi. A protein is encoded by the amylase gene.

Description

송이버섯으로부터 분리된 아밀라아제 유전자 및 상기 유전자로 엔코딩된 단백질{Amylase gene isolated from Tricholoma matsutake, and protein encoded thereby}Amylase gene isolated from Tricholoma matsutake, and protein encoded thereby

도 1a 내지 도 1b는 송이버섯에서 분리된 알파-아밀라아제 유전자의 염기서열 및 상기 유전자의 아미노산 서열에 관한 것이고,1a to 1b relates to the nucleotide sequence of the alpha-amylase gene isolated from the pine mushroom and the amino acid sequence of the gene,

도 2a 내지 도 2c는 송이버섯에서 분리된 글루코-아밀라아제 유전자의 염기서열 및 상기 유전자의 아미노산 서열에 관한 것이고,2a to 2c relates to the nucleotide sequence of the gluco-amylase gene isolated from the pine mushroom and the amino acid sequence of the gene,

도 3은 송이버섯 유래 알파-아밀라아제 유전자의 아미노산 서열과 다른 담자균류 유래 알파-아밀라아제 유전자의 아미노산 서열의 다상정렬 결과에 관한 것이고,Figure 3 relates to the result of polyphase alignment of the amino acid sequence of the pine mushroom-derived alpha-amylase gene and the amino acid sequence of other basidiomycete-derived alpha-amylase gene,

도 4는 송이버섯 유래 글루코-아밀라아제 유전자의 아미노산 서열과 다른 담자균류 유래 글루코-아밀라아제 유전자의 아미노산 서열의 다상정렬 결과에 관한 것이고,Figure 4 relates to the results of the multiphase alignment of the amino acid sequence of the pine mushroom-derived gluco-amylase gene and the amino acid sequence of other basidiomycete-derived gluco-amylase gene,

도 5는 pGEX-GAT 재조합 플라스미드이고,5 is a pGEX-GAT recombinant plasmid,

도 6은 과발현된 pGEX-GAT 재조합 단백질을 확인한 것이다.Figure 6 shows the overexpressed pGEX-GAT recombinant protein.

본 발명은 송이버섯에서 분리된 서열번호 1 또는 서열번호 2로 표시되는 아밀라아제 유전자 및 상기 유전자를 발현하는 단백질에 관한 것이다.The present invention relates to an amylase gene represented by SEQ ID NO: 1 or SEQ ID NO: 2 isolated from a pine mushroom and a protein expressing the gene.

아밀라아제는 아밀로오즈 및 아밀로펙틴과 같은 전분이나 글리코겐과 같이 α-결합의 글루코오스로 구성되어 있는 다당류에 작용한다. 아밀라아제는 작용하는 양식에 따라 α-amylase, β-amylase, glucoamylase의 3종으로 나뉜다. Amylases act on polysaccharides composed of α-linked glucose, such as starch or glycogen, such as amylose and amylopectin. Amylase is divided into three types, α-amylase, β-amylase and glucoamylase, depending on the mode of action.

α-amylase는 starch나 glycogen 등의 glucose 사슬을 안쪽에서 규칙성 없이 절단하여 반응의 초기부터 다당류는 급속히 저분자화 되어 요오드-starch 반응을 나타내지 않게 된다. β-amylase는 starch 나 glycogen 등의 glucose 사슬을 말단에서부터 차례로 순차적으로 maltose를 생성시키는 효소이다. α-amylase cleaves glucose chains such as starch and glycogen without regularity from the inside, and from the beginning of the reaction, polysaccharides rapidly become low molecular weight and do not show iodine-starch reaction. β-amylase is an enzyme that produces maltose sequentially from the ends of glucose chains such as starch or glycogen.

α-amylase, β-amylase는 둘 다 α-(1,4) 결합만을 분해하여 불규칙한 반응산물을 생성시키는 반면 amyloglucosidase라고도 불리는 glucoamylase는 starch 분자의 비환원성 말단으로부터 α-(1,4) 결합과 α-(1,6) 결합을 가수분해함으로써 규칙적으로 β-D-glucose를 생산하는 효소이다. α-amylase and β-amylase both degrade only α- (1,4) bonds to produce irregular reaction products, while glucoamylase, also called amyloglucosidase, binds α- (1,4) bonds and α from the non-reducing end of the starch molecule. It is an enzyme that regularly produces β-D-glucose by hydrolyzing-(1,6) bonds.

Glucoamylase 유전자는 지금가지 여러종류의 자낭균류와 담자균류에서 클론닝 되었는데 이들 유전자는 모두 N-terminal catalytic domain(CD)과 이어지는 threonine/serine(T/S)-rich linker, 그리고 C-terminal의 starch-binding domain(SBD)으로 구성된 3개의 domain이 보존되어 있음이 확인되었다. Glucoamylase genes have now been cloned in several types of streptococcus and basidiomycetes, all of which are N-terminal catalytic domains (CD) followed by threonine / serine (T / S) -rich linkers, and C-terminal starch- It was confirmed that three domains consisting of binding domains (SBDs) are preserved.

Amylase에 있어서 starch-binding domain(SBD)은 세가지의 역할이 알려져 있는데 불용성의 기질과 효소의 상호작용을 가능하게 하며, 기질을 catalytic domain(CD)의 active site로 운반하고, 어떤 경우에 있어서는 starch granule의 표면을 흐트리는 기능을 하는것으로 알려져 있다.The starch-binding domain (SBD) has three known roles in amylase, enabling the interaction of insoluble substrates with enzymes, transporting the substrate to the active site of the catalytic domain (CD), and in some cases starch granules. It is known to function to blur the surface.

α-amylase와 glucoamylase는 생물공학적인면에서도 중요한 역할을 하는 효소 중의 하나이다. glucoamylase는 glucose와 fructose의 산업적생산에 광범위하게 이용되고 있으며 또한 starch를 분해하여 얻은 당을 이용하여 ethanol을 생성하는데 amylase는 큰 잠재적 가능성을 가지고 있다. α-amylase and glucoamylase are one of the enzymes that play an important role in biotechnology. Glucoamylase is widely used in the industrial production of glucose and fructose, and amylase has great potential for producing ethanol from sugars obtained by breaking down starch.

α-amylase와 glucoamylase 관한 연구는 이들 유용유전자의 고발현을 통한 고생산은 물론 사용용도에 적합하도록 유전적인 엔지니어링을 통한 효율의 극대화 방법 등 여러 가지 분야에서 연구가 활발히 진행되고 있다.The research on α-amylase and glucoamylase has been actively conducted in various fields such as high production of these useful genes and methods of maximizing efficiency through genetic engineering to be suitable for use.

본 발명은 산업적으로 다양한 응용가치를 보유하여 큰 잠재적 이용 가능성을 가진 a-amylase와 glucoamylase 단백질을 코딩하는 유전자를 분리하기 위하여 소나무 뿌리에서 외생균근을 형성하여 생육하는 송이버섯 (Tricholoma matsutake)으로부터 cDNA library를 구축하고 α-amylase 와 glucoamylase 유전자를 클로닝하였다. α-amylase 와 glucoamylase 유전자의 클로닝을 위해 사용한 송이버섯은 국내 대구 근교의 가창 송림에서 채취하였다.The present invention provides a cDNA library from tricholoma matsutake, which forms and grows exogenous mycorrhiza on pine roots to isolate genes encoding a-amylase and glucoamylase proteins that have industrial potential and have great potential. And cloned the α-amylase and glucoamylase genes. Pine mushrooms used for the cloning of the α-amylase and glucoamylase genes were collected from Song-lim, Songchang, near Daegu, Korea.

아래에 실시한 예를 통하여 국내에서 채취된 송이버섯으로부터 α-amylase 와 glucoamylase 유전자의 클로닝을 확인할 수 있었고, 송이버섯 염색체 상에 존재하는 α-amylase 와 glucoamylase 유전자를 증폭하고 이를 클로닝하여 송이균 유래의 α-amylase 와 glucoamylase을 산업적으로 활용할 수 있는 기초적인 시스템을 개발하였다. Through the following examples, cloning of α-amylase and glucoamylase genes could be confirmed from pine mushrooms collected in Korea, and the α-amylase and glucoamylase genes present on the pine mushroom chromosome were amplified and cloned. We have developed a basic system to industrially use amylase and glucoamylase.

본 발명의 핵심은 국내 자생의 최고품질의 송이버섯으로부터 α-amylase 와 glucoamylase 유전자를 분리하고, α-amylase 와 glucoamylase 유전자를 클로닝하였으며, 본 연구에서 증폭한 송이버섯 유래의 α-amylase 와 glucoamylase 유전자의 염기서열을 기존에 보고된 다양한 종류의 α-amylase 와 glucoamylase 유전자와 비교할 때, 송이버섯 유래의 특이한 α-amylase 와 glucoamylase임을 확인하였고 다른 담자균류에서 기존에 보고된 α-amylase 와 glucoamylase와는 다른 a-amylase 와 glucoamylase임을 유전자의 염기서열과 아미노산의 배열로 확인할 수 있었다. The core of the present invention is to isolate the α-amylase and glucoamylase genes from the highest quality pine mushrooms in Korea, clone the α-amylase and glucoamylase genes, and amplify the α-amylase and glucoamylase genes from the mushrooms amplified in this study. Comparing the nucleotide sequences with various previously reported α-amylase and glucoamylase genes, it was confirmed that they are unique α-amylase and glucoamylase derived from pine mushrooms, and a- Amylase and glucoamylase were identified by the gene sequence and amino acid sequence.

본 발명은 a-amylase와 glucoamylase를 송이버섯으로부터 클로닝하여 확인하고, a-amylase와 glucoamylase 유전자의 염기서열을 해명하였다. 또한 송이버섯의 a-amylase와 glucoamylase을 상업적 용도로 이용할 수 있는 기반을 마련하였다.The present invention was confirmed by cloning a-amylase and glucoamylase from matsutake mushrooms and elucidated the nucleotide sequences of a-amylase and glucoamylase genes. In addition, a-amylase and glucoamylase of Matsutake mushrooms were prepared for commercial use.

산업적으로 많이 이용되고 있는 a-amylase 및 gluco-amylase를 코딩하는 새로운 유전자를 국내에서 채취한 송이버섯(Tricholoma matsutake)에서 클로닝하였다. 송이버섯 유래의 a-amylase 및 gluco-amylase 단백질과 관련된 유전자를 확보하기 위하여 송이버섯으로부터 총 RNA (total RNA)를 분리·정제하였으며, 이들의 double stranded cDNA를 합성하고 cDNA 라이브러리를 제작하여 송이버섯 (Tricholoma matsutake) 유전체에 coding 되어 있는 a-amylase 와 gluco-amylase 유전자를 cDNA library로부터 스크리닝 하여 a-amylase 와 gluco-amylase 유전자의 염기서열을 분석하였다. New genes encoding a-amylase and gluco-amylase, which are widely used in industry, were cloned from Tricholoma matsutake collected in Korea. In order to secure genes related to a-amylase and gluco-amylase proteins derived from pine mushrooms, total RNA was isolated and purified from pine mushrooms, double stranded cDNAs were synthesized, and cDNA libraries were prepared. A-amylase and gluco-amylase genes encoded in the Tricholoma matsutake genome were screened from the cDNA library to analyze the nucleotide sequences of the a-amylase and gluco-amylase genes.

따라서, 본 발명은 서열번호 1 또는 서열번호 2로 표시되는 아밀라아제 유전자를 제공하며, 상기 아밀라아제가 알파-아밀라아제 또는 글루코-아밀라아제에서 선택된 하나이다. 특히, 상기 유전자가 유용 토착 사상균을 포함한 송이버섯으로부터 분리될 수 있다.Accordingly, the present invention provides an amylase gene represented by SEQ ID NO: 1 or SEQ ID NO: 2, wherein the amylase is one selected from alpha-amylase or gluco-amylase. In particular, the gene can be isolated from matsutake mushrooms containing useful native filamentous fungi.

또한, 본 발명은 서열번호 1 또는 서열번호 2로 표시되는 아밀라아제 유전자로 엔코딩된 단백질을 제공한다.The present invention also provides a protein encoded by the amylase gene represented by SEQ ID NO: 1 or SEQ ID NO: 2.

이하, 본 발명을 좀 더 구체적으로 살펴보면 다음과 같다.Hereinafter, the present invention will be described in more detail.

본 발명은 a-amylase와 glucoamylase 유전자를 이용하여 생산된 a-amylase와 glucoamylase 유전자 산물을 이용하여 화장품산업, 양조산업 및 의료용 산업의 소재로 직접 응용 가능하다. The present invention can be directly applied to materials of the cosmetic industry, brewing industry and medical industry using a-amylase and glucoamylase gene products produced using the a-amylase and glucoamylase genes.

본 발명은 하기의 실험예에 의하여 보다 명확히 이해될 수 있으며, 하기의 실험 예는 본 발명의 예시 목적에 불과하며 발명의 영역을 제한하거나, 본 발명의 내용이 여기에 한정되는 것은 아니다. The present invention can be more clearly understood by the following experimental examples, the following experimental examples are only for the purpose of illustrating the invention and limit the scope of the invention, or the content of the present invention is not limited thereto.

실험예 1: 송이버섯으로 제작한 cDNA library로부터 클론닝한 a-amylase 와 glucoamylase 유전자의 염기배열과 아미노산의 배열 Experimental Example 1: Nucleotide sequence and amino acid sequence of a-amylase and glucoamylase genes cloned from cDNA library prepared with pine mushroom

국내 대구 근교의 가창 송림에서 채취한 송이버섯으로부터 QIAGEN의 RNeasy kit를 이용하여 total RNA를 분리,정제하고 RT-PCR반응으로 1st cDNA를 합성하였다. 1st cDNA를 주형으로 다시 PCR하여 final cDNA를 만들고 벡터에 삽입하고 이를 electroporation 하여 cDNA library를 제작하였다. 그리고 Seq I sequencing primer를 이용하여 각각의 클론을 sequencing하고 그 결과 도 1에 나타난 서열번호 1의 유전자와 도 2에 나타난 서열번호 2의 유전자를 발견하였다.Total RNA was isolated and purified from matsutake mushrooms in Songchang, Korea near Daegu using QIAGEN's RNeasy kit and synthesized 1st cDNA by RT-PCR reaction. PCR was performed again on the 1st cDNA template to make a final cDNA, inserted into a vector and electroporation to prepare a cDNA library. Sequencing each clone using Seq I sequencing primer and found the gene of SEQ ID NO: 1 shown in Figure 1 and the gene of SEQ ID NO: 2 shown in FIG.

이러한 유전자들을 이용하여 NCBI에서 BLAST SEARCH를 한 결과, α-amylase와 glucoamylase 유전자와 높은 상동성을 나타냄을 확인할 수 있었다.BLAST SEARCH in NCBI using these genes showed high homology with α-amylase and glucoamylase genes.

실험예 2 : Clustal X 프로그램을 이용한 담자균류의 a-amylase 와 glucoamylase 유전자 아미노산 서열과 송이버섯으로부터 분리한 a-amylase와 glucoamylase 유전자의 아미노산 서열의 다상정렬 (multiple-alignment) 결과. Experimental Example 2: Multiple-alignment results of the a-amylase and glucoamylase gene amino acid sequences of basidiomycetes and the amino acid sequences of the a-amylase and glucoamylase genes isolated from pine mushrooms using the Clustal X program.

송이버섯으로부터 분리한 a-amylase 와 glucoamylase 유전자의 아미노산 서열과 다른 담자균류에서 분리된 a-amylase와 glucoamylase 유전자 아미노산 서열을 Clustal X 프로그램을 이용하여 다상정렬 (multiple-alignment) 결과는 도 3 및 도 4와 같고, glucoamylase 유전자의 큰 특징중의 하나인 N-terminal에서 catalytic domain인 5개의 보존적인 영역이 발견되었고, C-terminal에서는 보존영역인 Starch Binding Domain (SBD)가 발견되었다. a-amylase에서 또한 4개의 보존영역을 확인할 수 있었다.The results of multiple-alignment of the amino acid sequences of the a-amylase and glucoamylase genes isolated from pine mushrooms and the amino acid sequences of the a-amylase and glucoamylase genes isolated from other basidiomycetes using the Clustal X program are shown in FIGS. 3 and 4. In the N-terminal, one of the major features of the glucoamylase gene, five conserved regions, the catalytic domain, were found, while the C-terminal, the Starch Binding Domain (SBD), was found. In the a-amylase, four conserved regions were also identified.

실험예 3 : Pichia pastoris 에서의 pGEX-GAT recombinant protein의 발현 Experimental Example 3: Pichia Expression of recombinant protein in a pGEX-GAT pastoris

클론닝 된 glucoamylase cDNA를 pGEX vector에 클론닝하여 도 5와 같은 pGEX-GAT 재조합 plasmid를 제작한 후 Pichia pastoris에 transformation하였다. Transformant 중 positive clone을 selection하여 0.5%의 methanol로 induction하여 도 6과 같이 이들의 total protein을 확인하였다.The cloning of the glucoamylase cDNA and 5 by cloning in pGEX vector pGEX-GAT After the fabrication of the recombinant plasmid Pichia Transformed to pastoris . Positive clones of the transformants were selected and induced with 0.5% methanol to confirm their total protein as shown in FIG. 6.

본 발명에 따른 알파-아밀라아제 유전자와 글루코아밀라아제 유전자를 이용하여 생산한 유전자 산물을 이용하여 화장품산업, 양조산업 및 의료용 산업의 소재로 직접 응용 가능하다. The gene product produced using the alpha-amylase gene and the glucoamylase gene according to the present invention can be directly applied to materials of the cosmetic industry, the brewing industry and the medical industry.

서열목록 전자파일 첨부 Attach sequence list electronic file  

Claims (4)

서열번호 1 또는 서열번호 2로 표시되는 아밀라아제 유전자.Amylase gene represented by SEQ ID NO: 1 or SEQ ID NO: 2. 제 1항에 있어서, 상기 아밀라아제가 알파-아밀라아제 또는 글루코-아밀라아제에서 선택된 하나인 것을 특징으로 하는 아밀레이즈 유전자.The amylase gene according to claim 1, wherein the amylase is one selected from alpha-amylase or gluco-amylase. 제 1항 또는 제 2항에 있어서, 상기 유전자가 유용 토착 사상균을 포함한 송이버섯으로부터 분리된 것을 특징으로 하는 아밀레이즈 유전자.The amylase gene according to claim 1 or 2, wherein the gene is isolated from a pine mushroom including useful native filamentous fungi. 서열번호 1 또는 서열번호 2로 표시되는 아밀라아제 유전자로 엔코딩된 단백질.A protein encoded by the amylase gene represented by SEQ ID NO: 1 or SEQ ID NO: 2.
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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
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