• Journal of Microbiology and Biotechnology
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• v.3 no.2
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• pp.78-85
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• 1993

In order to elucidate the mechanism which regulates the production of cyclodextrin glucanotransferase (CGTase) and to achieve overproduction of CGTase by releasing catabolite (glucose) repression, several catabolite repression resistant mutants were selected from newly screened Bacillus firmus var. alkalophilus H609, after NTG (N-methyl-N -nitro-N-nitrosoguanidine) treatment, using 2-deoxyglucose as a nonmetabolizable analog of catabolite glucose and as a selection marker. Five catabolite repression resistant mutants were selected from about 30, 000 2-deoxyglucose resistant colonies. Relative catabolite repression indices of the selected mutants were in the range of 8~80% assuming 100% for parent strain. The amount of CGTase produced by the mutant strain CR41, which was 250 units/ml, was three times larger than that produced by its parent strain. The mutation seems to have occurred in the regulatory region of CGTase gene and not in the structural region or the glucose transporting system in cell membrane. The enzymatic properties of CGTase excreted from parent and mutant strains were also compared.

• Microbiology and Biotechnology Letters
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• v.18 no.6
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• pp.566-570
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• 1990

Regulation of $\beta$ -galactosidase formation was studied with Lactobacillus sporogenes. Synthesis of the enzyme was effectively induced by isopropyl- $\beta$-D-thiogalactopyranoside (IPTG) or galactose, and to a much lower level by lactose. When 15 mM glucose was added at the different intervals to the cultures that had been in contact with IPTG, the same levels of inhibition of the enzyme synthesis were observed (approximately one-third the differential rate of a control culture without glucose). This suggests that glucose did not interfere with the entry of the inducer into the cells, but interfere with the formation of $\beta$ -galactosidase through catabolite repression. The glucose inhibitory effect was not overcome by adding CAMP or cGMP to the culture media.

• Microbiology and Biotechnology Letters
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• v.14 no.4
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• pp.293-298
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• 1986

Sisomicin, which is one of aminoglycoside antibiotics, was produced by Micromonospora inyoensis. The effects of carbon sources on sisomicin production were studied in batch cultures. Starch, dextrin and maltose were good carbon sources for the production of sisomicin. However, when glucose was used, the antibiotic productivity decreased significantly due to a carbon catabolite regulation. The carbon catabolite regulation depends mostly on carbon catabolite repression, but not on carbon catabolite inhibition. On the other hand, the growth-production curves of batch cultures show that sisomicin is produced most actively during the idiophase.

• Microbiology and Biotechnology Letters
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• v.24 no.2
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• pp.137-142
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• 1996

The biosynthesis and catabolite repression of cyclodextrin glucanotransferase(CGTase) and cyclodextrinase(CDase) were studied in Bacillus sp. KJI6. In accompanying to the cell growth, CGTase was synthesized during early growth phase (20h culture) and CDase was synthesized during late growth phase (60h culture). Synthesis of CGTase was rather constitutive than that of CDase in the absence or presence of carbon source. Production of CDase was strongly stimulated by amylopectin and $\gamma$-CD medium (about 6 times), but CGTase synthesis was slightly increased (about 1.3 times). Easily metabolizable carbohydrates such as D-glucose, D- fructose and D-mannose completely repressed the expression of CDase, whereas their repressive effect to CGTase synthesis was relatively negligible. By addition of 10 mM cAMP, any significant effect on the synthesis of the two enzymes was not observed. Hardly metabolizable glucose analogues such as 2-deoxy-D-glucose and 3-0-methyl-D-glucopyranose also did not show any repression on the syntheses of CGTase and CDase. This indicates that D-glucose has to be metabolized to exert its repressive effect. With these results, it seems likely that the biosynthesis of CGTase and CDase are regulated by the catabolite repression due to unknown metabolite(s) of EM pathway.

• Microbiology and Biotechnology Letters
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• v.21 no.6
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• pp.549-555
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• 1993

The production of cellulase by Pseudomonas sp. LBC505 isolated was under the strict genetic and biochemical control mechanisms such as catabolit repression and induction. These biochemical control reduced cellulase production. Thus LBC505 was mutated to increase enzyme yields. Cells growth and cellulase production were inhibited by the addition of 2-deoxy glucose (2-DG), which is presumed to function as repressor for the selection of high cellulase yielding mutant.

• KSBB Journal
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• v.7 no.4
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• pp.265-270
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• 1992

Low cost fermentation substrates frequently contain a mixture of carbon sources including hexoses, pentoses and disaccharides. Fermentation of such mixtures requires an understanding of how each of these substrates is utilized. During batch culture of Pichia stipitis CBS 5776 on sugar mixtures, glucose causes catabolite repression of xylose and cellobiose utilization. Also, glucose causes a permanent repression of xylose utilization as evidenced by reduced growth rates during the xylose phase of glucose/xylose fermentation. The growth model for multiple substrates is developed based on a cyclic AMP mediated catabolite repression mechanism and this model adequately described the growth and ethanol production from sugar mixtures.

• Journal of Microbiology and Biotechnology
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• v.11 no.1
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• pp.131-137
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• 2001

Previous work has identified that only the catabolite responsive element A (creA; previously called cre-2) out of two potential cre sequences (cre-1: nucleotide +160 to +173 and cre-2: +173 to +186), recognized within the coding region of the xylanaseA gene (xynA) of Bacillus stearothermophilus No.236, was actually, was actually involved in the carbon catabolite repression(CCR) of xynA expression in B. subtilis. However, the level of CCR of xynA expression in the original B.stearothermophilus No.236 strain (70-fold repression). Therefore, to search for an additional cre element in the promoter region, the upstream region of the xynA gene was subcloned by chromosome walking, and as a result, another potential cre element (nucleotide -124∼-137; designated creB) was recognized in this region. The cre-like sequence revealed a high homology to the cre consensus sequence. The xylanase activity of B. subtilis MW15 bearing pWPBR14 (containing creA and creB) cultured in a medium containing xylose as the sole carbon source was about 7.7 times higher than that observed for the same culture containing glucose. B. subtilis MW15 bearing pWPBR23 (containing only creA) produced an activity about 2.4 times higher. This pattern of CCR was confirmed using derivatives of xynA::aprA fusion plasmids. Furthermore, a measurement of the amounts of the xynA transcript showed a similar pattern as that for the production of xylanase. In addition, the synthesis of xylanase in B. subtilis QB7115 [a catabolite control protein A (ccpA) mutant strain] carrying pWPBR14 was almost completely relieved from glucose repression. Together, these results lead to a conclusion that the CCR of the expression of the xynA gene is mediated by CcpA binding at creA and creB sites in B. subtilis.

• Microbiology and Biotechnology Letters
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• v.29 no.2
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• pp.72-77
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• 2001

Expression of f3 ~agarase Gene and Catabolite Repression in Escherichia coli by the Promoter of Alginate Lyase Gene Isolated from Marine Pseudomonas sp. Jin, Cheal~Ho, J~Hyeon Park, Jeong-Hyun Han, YoonM Hyeok Chae, Jong~Hee Lee, Jung-Kee Lee!, and In-800 Kong*. Faculty of Food Science and Biotechnology, Pukyong National UniversitYt Pusan 608-737, Korea, llnBioNet Co. 1690-3 Taejon 306-230, Korea - Promoter is a key factor for expression of the recombinant protein. There are many promoters for overexpression of protein in various organisms. The aly promoter of Pseudomonas sp. W7 isolated from marine environment was known to be a constitutive expression promoter of the alginate lyase gene, and it's promoter activity is repressed by glucose in Escherichia coli. To investigate the catabolite repression of the aly promoter ~md association between the promoter mutants, f3 agarase gene, which was also cloned from Pseudomonas sp. W7 was connected to the aly promoter with the sequence the coding 46 N-terminal amino acids ofthe alginate lyase gene. The constructed plasmid was introduced into E. coli and the agarase activity was measured. Fourty six amino acids of the alginate lyase gene was serially deleted using peR to the direction of 5' upstream region and subcloned. The agarase was overexpressed by the aly promoter and the production of agarase was repressed by the addition of glucose into culture media. Fourty six amino acids of alginate lyase did not affect the production of agarase at all. The deletion of a putative stem-loop structure in the aly promoter induced the decrease of f3 -agarase productivity.

• Journal of Microbiology and Biotechnology
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• v.8 no.1
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• pp.21-27
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• 1998

The xylA gene of Bacillus stearothermophilus encoding the major ${\beta}$-xylosidase was previously cloned and sequenced. In the present study we examined the regulation of the cloned xylA gene expression in Bauillus subtilis MW15 carrying the xylA::aprA fusion plasmids. The induction of the fused xylA gene expression remained uninfluenced by any of the carbon sources tested but the gene expression was repressed about 2-3 fold in the presence of glucose. Two CRE-like sequences (CRE-1: nucleotides ＋ 124 to ＋136 and CRE-2: ＋247 to ＋259) were recognized within the reading frame region of the xylA gene. The deletion experiments showed that the CRE-2 sequence had a role in catabolite repression (CR) as a true CRE of the xylA gene, but the CRE-1 had no effect on CR of the xylA gene expression. Surprisingly, the deletion of the CRE- 1 sequence reduced about 2~3 fold of the expression of the xylA fused gene. The repression ratios of the xylA gene expression were estimated to be about 0.4 from the assay of subtilisin activity, and about 0.3 at the level of transcription by determining the amounts of xylA transcripts in B. subtilis. While, the level of CR of the xylA gene was assessed to be about l0-fold in previous work when the relative amounts of the xylA transcripts were measured in B. stearothermophilus.

• The Journal of Natural Sciences
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• v.18 no.1
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• pp.29-38
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• 2007

Regulation of invertase biosynthesis was studied with alkalophilic and thermophilic Bacillus cereus TA-11. Biosynthesis of invertase in Bacillus cereus TA-11 was effectively induced in the presence of 10 mM of sucrose for 180 min and 25 mM of raffinose for 90 min, respectively. Glucose repressed the invertase induction by sucrose and as late addition time of glucose, invertase formation was increased, indicating that glucose repression was occurred by inducer exclusion. Catabolite repression was not reduced by the addition of cAMP for 180 min of induction.