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WO2002031119A1 - Mutant resistant a la repression catabolique - Google Patents

Mutant resistant a la repression catabolique Download PDF

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Publication number
WO2002031119A1
WO2002031119A1 PCT/KR2000/001147 KR0001147W WO0231119A1 WO 2002031119 A1 WO2002031119 A1 WO 2002031119A1 KR 0001147 W KR0001147 W KR 0001147W WO 0231119 A1 WO0231119 A1 WO 0231119A1
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WO
WIPO (PCT)
Prior art keywords
bacillus thermoglucosidasius
glucose
strain
strains
catabolite repression
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/KR2000/001147
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English (en)
Inventor
Bon-Tag Koo
Kee-Don Park
Jin-Man Kim
Jung-Ki Lee
Guk-Jin Kim
Hyun-Kuk Kim
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Inbionet Corp
Original Assignee
Inbionet Corp
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Inbionet Corp filed Critical Inbionet Corp
Priority to PCT/KR2000/001147 priority Critical patent/WO2002031119A1/fr
Priority to AU2000279668A priority patent/AU2000279668A1/en
Publication of WO2002031119A1 publication Critical patent/WO2002031119A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • 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.)
    • C12N9/2417—Alpha-amylase (3.2.1.1.) from microbiological source
    • 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
    • C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20—Bacteria; Culture media therefor
    • C12N1/205—Bacterial isolates
    • 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
    • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
    • 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)
    • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12R—INDEXING SCHEME ASSOCIATED WITH SUBCLASSES C12C - C12Q, RELATING TO MICROORGANISMS
    • C12R2001/00—Microorganisms ; Processes using microorganisms
    • C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
    • C12R2001/07—Bacillus

Definitions

  • the present invention relates to novel Bacillus strains that can produce industrially useful enzymes. More particularly, the present invention relates to the catabolite repression insensitive mutants of thermophihc Bacillus thermoglucosidasius with mutated glucose transport system and the processes for preparation and application thereof.
  • Amylase and cellulase have been utilized most frequently for industrial uses.
  • Starch and cellulose can be decomposed into bioavailable sugars by degrading with bacterial enzymes and be utilized by the microorganism.
  • the object of the present invention is to provide catabolite repression insensitive Bacillus strains producing amylase and cellulase specifically, which can improve the enzyme productivity as well as save on glucose for secondary fermentation.
  • the present invention provides amylase and cellulase producing Bacillus thermoglucosidasius strains, which are made by damaging the repression mechanism of the enzymes and by destroying artificially the main bacterial mechanism of glucose absorption through gene mutation technique.
  • the present invention provides the mutant strain, Bacillus thermoglucosidasius BtgMul (KCCM-10221) producing amylase, and the mutant strain, Bacillus thermoglucosidasius BtgcelMul (KCCM-10220) producing cellulase which are damaged in the catabolite repression process and are inhibited in glucose uptake process due to the destruction of glucose transport system.
  • the above mutant Bacillus thermoglucosidasius strains can be prepared by the processes comprising steps as follows:
  • the present invention provides a method for producing the amylase or the cellulase by using the Bacillus thermoglucosidasius strains obtained above.
  • the present invention provides a method for decomposing food waste by using the above Bacillus thermoglucosidasius mutants.
  • the mutant Bacillus thermoglucosidasius strains are separated according to the methods described below. N-methyl-N'-nitro-N- nitrosoguanidine (NTG) and ultraviolet ray is treated for mutating thermophilic Bacillus thermoglucosidasius strains. Then the mutant strains are selected by using culture medium containing 2-deoxyglucose. The mutant strains obtained above is cultivated again for 22 to 26 hours in Nutrient agar medium (beef extract 0.3%>; peptone 0.5%>), which contains 0.3% of glucose, 1.0% of starch or cellulose. The above agar plate is dyed with 0.1 N of iodide solution or Congo-Red reagent. Finally, catabolite repression insensitive Bacillus mutants are distinguished by clearness, and collected from the colonies forming transparent circles.
  • NTG N-methyl-N'-nitro-N- nitrosoguanidine
  • ultraviolet ray is treated for mutating thermophilic Bacillus thermoglucosi
  • the Bacillus thermoglucosidasius strain which loses the cellulase activity of the wild type and shows insensibility to catabolite repression of amylase are selected among the above mutant strains.
  • Bacillus thermoglucosidasius which loses the amylase activity of the wild type strain and sustains the insensibility to catabolite repression of cellulase are also selected among the above mutant strains.
  • mutant strains of the present invention are observed to increase the activities of amylase and cellulase remarkably when the two mutants are co-cultured in Nutrient medium.
  • the peculiar competition between the mutant Bacillus thermoglucosidasius strains might not exist since the two strains that derived from the same parental strain have similar physiological property.
  • the activity of amylase in the medium plate is measured by the process mentioned below.
  • the sample Bacillus strain is cultivated in Nutrient agar medium containing 1.0% of starch, and is dyed onto medium plate by 0.1 N solution of iodide in order to make transparent circles. Then the radius of the transparent circles is measured.
  • the enzyme activity of cellulase in the medium plate is measured by the process described below.
  • the sample Bacillus strain is cultivated in Nutrient agar medium containing 1.0% of cellulose, and is dyed by 0.1%) of Congo-Red reagent. After washing the strain with 1 N solution of sodium chloride, the radius of the transparent circles is determined.
  • the activities of amylase and cellulase are measured by the process as follows. 100 ⁇ l of the bacterial culture supernatant (containing enzyme) is added to 900 ⁇ l solution of 0.1 %> starch or 1% cellulose, and is reacted at 55°C for 30 minutes. Then the same volume of dinitrosalicylic acid (DNS) solution is mixed, and the mixture is boiled for 15 minutes. The absorbance of the sample is measured at 570 nm. In the comparative sample, 100 ⁇ l of sterilized water is utilized instead of the enzyme supernatant. In the above process, unit is defined as enzyme amount showing 0.001 difference of the absorbance value from that of the comparative sample excluding enzymes
  • Fig. 1 represents the activities of the catabolite repression insensitive mutants of the present invention, Bacillus thermoglucosidasius BtgMul (KCCM-
  • KCCM- 10220 Bacillus thermoglucosidasius BtgcelMul showing specific activities for the amylase and cellulase respectively; in Nutrient agar plate containing 1% of starch (Fig. 1A); in Nutrient agar plate containing 1%> of starch and 0.3% of glucose (Fig. IB); in Nutrient agar plate containing 1%> of CMC (Fig. IC); and in Nutrient agar plate containing 1% of CMC and 0.3% of glucose (Fig. ID).
  • Fig. 2 represents the mutant Bacillus thermoglucosidasius strain damaged in the group translocation process, main glucose transporter, which is separated by using 2-deoxyglucose.
  • Fig. 3 represents the growth curves of the wild type Bacillus thermoglucosidasius and catabolite repression insensitive Bacillus thermoglucosidasius BtgMul (KCCM-10221) and Bacillus thermoglucosidasius BtgcelMul (KCCM-10220), which are cultivated in glucose condition.
  • Fig. 4 represents the amylase activities of the wild type Bacillus thermoglucosidasius and catabolite repression insensitive Bacillus thermoglucosidasius BtgMul (KCCM-10221) and Bacillus thermoglucosidasius BtgcelMul (KCCM-10220), which are cultivated in the Nutrient medium containing starch as a carbon source.
  • Fig. 5 represents the cellulase activities of the wild type Bacillus thermoglucosidasius and the catabolite repression insentive Bacillus thermoglucosidasius BtgMul (KCCM-10221) and Bacillus thermoglucosidasius BtgcelMul (KCCM-10220), which are cultivated in the Nutrient medium containing cellulose as a carbon source.
  • KCCM-10221 Bacillus thermoglucosidasius BtgMul
  • KCCM-10220 Bacillus thermoglucosidasius BtgcelMul
  • Fig. 7 represent the food waste weight reduction ratio of the catabolite repression insensitive Bacillus thermoglucosidasius BtgMul (KCCM-10221) (Fig. 7 A) and the number of catabolite repression insensitive Bacillus thermoglucosidasius BtgMul (KCCM-10221) (Fig. 7B) when applied to food waste volume reduction equipment.
  • Fig. 8 represent the productivities of the amylase (Fig. 8A) and cellulase (Fig. 8B) when Bacillus thermoglucosidasius BtgMul and Bacillus thermoglucosidasius BtgcelMul strains (KCCM-10221 and KCCM-10220) are co-cultured.
  • Preferred Embodiment 1 Mutation of microorganism Bacillus thermoglucosidasius (KCTC accession number 3400 BP) was obtained from the gene bank of KRIBB (Korea Research Institute of Bioscience and Biotechnology; #52 Oun-dong, Yusong-ku, Taejon 305-333) and was cultured by using 5 ⁇ l of Nutrient medium (beef extract 0.3%; peptone 0.5%o) in 55°C for 24 hours. Then NTG (N-methyl-N'-nitro-N-nitrosoguanidine) was added toward 1 mM, and the above strain was cultivated by shaking for 2 more hours. The culture medium was recovered and smeared onto the Nutrient agar medium containing 1%> of starch or cellulose by using the successive dilution smear method.
  • mutant strains obtained above were inoculated onto Nutrient agar medium containing 0.3% of glucose, 1% of starch or cellulose, and were cultivated for 24 hours. Then 0.1 N of iodide solution or 0.1 % of Congo-Red solution was treated so as to select the catabolite repression insensitive mutant which existed in the transparent circle -of the largest radius and represented the specific enzyme activity of amylase or cellulase independently.
  • the mutant strains obtained above were named BtgcelMul and BtgMul respectively.
  • the Bacillus thermoglucosidasius BtgcelMul and Bacillus thermoglucosidasius BtgMul strains have been deposited with Corporation Korean Culture Center of Microorganism, Seoul, Korea, on Apr. 2, 1999 (accession number: KCCM-10220; KCCM-10221 respectively).
  • the enzyme activity variation against glucose was depicted in Table 1.
  • the wild type Bacillus thermoglucosidasius and the mutant Bacillus thermoglucosidasius BtgcelMul (KCCM-10221) and BtgcelMul (KCCM-10220) were inoculated with 0.1% into Nutrient medium containing O.P/o of starch or cellulose and 0.3% of glucose respectively, and cultured at 55°C by shaking. The growth of the Bacillus thermoglucosidasius strains was observed at 8-hour interval.
  • Bacillus thermoglucosidasius BtgcelMul (KCCM-10221) and BtgcelMul (KCCM- 10220)
  • Bacillus thermoglucosidasius BtgcelMul (KCCM-10221) and BtgcelMul (KCCM- 10220)
  • the enzyme productivities of the Bacillus thermoglucosidasius strains were observed at 8-hour interval.
  • the wild type increased the amylase activity for absorbing glucose from culture medium until catabolite repression was worked due to glucose accumulation.
  • the mutant Bacillus thermoglucosidasius BtgMul (KCCM-10221) augmented the enzyme productivity consistently although glucose concentration increased. The results were depicted in Fig. 4.
  • Bacillus thermoglucosidasius BtgMul (KCCM-10221) and BtgcelMul (KCCM-10220)
  • Bacillus thermoglucosidasius BtgMul (KCCM-10221) and BtgcelMul (KCCM-10220)
  • the enzyme productivities of the Bacillus thermoglucosidasius strains were measured at 8-hour interval.
  • the wild type reduced the enzyme productivity through catabolite repression since glucose was accumulated.
  • the mutant Bacillus thermoglucosidasius BtgcelMul (KCCM-10220) increased the enzyme productivity consistently according to time. The results were depicted in Fig. 5.
  • Preferred Embodiment 6 Concentration variation of glucose in the medium of the mutant strains during fermentation
  • Bacillus thermoglucosidasius BtgMul (KCCM-10221) and BtgcelMul (KCCM- 10220)
  • KCCM-10221 and BtgcelMul (KCCM- 10220)
  • the concentration variation of the Bacillus thermoglucosidasius strains was observed at 8-hour interval.
  • the wild type strain has consumed glucose rapidly in liquid medium.
  • both the mutant Bacillus thermoglucosidasius accumulated glucose. The data was depicted in Fig. 6.
  • Preferred Embodiment 7 Application of the mutant strains for developing equipment of food waste volume reduction
  • the each cell number of the mutant strains within the reactor was measured by using Nutrient agar medium containing final 30 mM concentration of 2-deoxyglucose and 1%> of starch or cellulose.
  • the mutant Bacillus thermoglucosidasius BtgMul (KCCM-10221) was identified to be a major population.
  • the detailed data was shown in Fig. 7B.
  • Preferred Embodiment 8 Increase of ⁇ he enzyme activity in co-culture of the mutant Bacillus thermoglucosidasius strains
  • the mutant Bacillus thermoglucosidasius BtgMul shows catabolite repression insensibility specific for amylase, and is damaged in group translocation mechanism. Hence, the mutant represented high amylase activity in Nutrient agar medium containing 0.3% of glucose.
  • Bacillus thermoglucosidasius BtgcelMul showing the catabolite repression insensibility specific for cellulase represented high cellulase activity in Nutrient agar medium containing 0.3%) of glucose.
  • the mutant Bacillus thermoglucosidasius BtgMul (KCCM-10221) and BtgcelMul (KCCM-10220) were multiplied to 2.3 x 10 8 and 6.5 x 10 7 CFU/ml respectively in Nutrient medium containing O.P/o of starch or cellulose and 0.3 % of glucose, which was the higher growth rate than 6.2 x 10 7 CFU/ml of the wild type.
  • the amylase activity of Bacillus thermoglucosidasius BtgMul increased continuously during 48 to 56 hours culture.
  • the enzyme activity of the wild type Bacillus thermoglucosidasius reduced on account of glucose effect. Approximately, the enzyme activity of the mutant Bacillus thermoglucosidasius BtgMul was more than six times of the highest activity of the wild type.
  • the cellulase activity of the mutant Bacillus thermoglucosidasius BtgMul was approximately more than twice as high as that of the wild type strain.
  • the glucose concentration of medium was decreased consistently in the wild type consuming glucose, but the glucose concentration increased to 4.5 g/1 of maximum value in the mutant Bacillus thermoglucosidasius BtgMul (KCCM-10221) and BtgcelMul (KCCM-10220) culture, which described the glucose accumulation toward 1.5 times of the initial concentration.
  • the mutant strain was inoculated with 1,000 ppm amount of the total food waste weight into food waste volume reduction equipment. Then 1 kg of new food waste was added daily and was adjusted for about 1 week. Resultantly, the number of live bacteria increased toward more than 10 CFU/ml and the total mass reduction ratio reached 140%> approximately.
  • the mutant Bacillus thermoglucosidasius BtgMul and BtgcelMul co-cultured in the same medium shows about 1.6 times and 1.4 times activities of amylase and cellulase than those cultured independently.

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Abstract

Souches thermophiles résistantes à la répression catabolique de Bacillus thermoglucosidasius BtgMul (KCCM-10221) produisant de l'enzyme amylolytique et de Bacillus thermoglucosidasius BtgclMul (KCCM-10220) produisant de la cellulase. Etant donné que la coculture de ces deux souches, BtgMul et BtgcelMul, augmente considérablement l'activité de l'enzyme amylolytique et de la cellulase, ces deux souches pourraient être appliquées au processus de réduction du volume des déchets alimentaires du fait qu'elles réduisent fortement le volume des déchets alimentaires.
PCT/KR2000/001147 2000-10-13 2000-10-13 Mutant resistant a la repression catabolique Ceased WO2002031119A1 (fr)

Priority Applications (2)

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PCT/KR2000/001147 WO2002031119A1 (fr) 2000-10-13 2000-10-13 Mutant resistant a la repression catabolique
AU2000279668A AU2000279668A1 (en) 2000-10-13 2000-10-13 Mutant resistant to catabolite repression

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Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR101262152B1 (ko) 2010-06-22 2013-05-14 한국생산기술연구원 이타콘산 고생산성 변이 균주, 이의 제조 방법 및 이를 이용한 이타콘산의 생산 방법

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6426980A (en) * 1987-07-23 1989-01-30 Nec Corp Circuit differential extracting device
US5079154A (en) * 1988-03-30 1992-01-07 Kao Corporation Mutant resistant to cell membrane synthesis inhibitor and process for preparing the same
US6011147A (en) * 1986-04-30 2000-01-04 Rohm Enzyme Finland Oy Fungal promoters active in the presence of glucose

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6011147A (en) * 1986-04-30 2000-01-04 Rohm Enzyme Finland Oy Fungal promoters active in the presence of glucose
JPS6426980A (en) * 1987-07-23 1989-01-30 Nec Corp Circuit differential extracting device
US5079154A (en) * 1988-03-30 1992-01-07 Kao Corporation Mutant resistant to cell membrane synthesis inhibitor and process for preparing the same

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR101262152B1 (ko) 2010-06-22 2013-05-14 한국생산기술연구원 이타콘산 고생산성 변이 균주, 이의 제조 방법 및 이를 이용한 이타콘산의 생산 방법

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