• Food Science and Preservation
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• v.22 no.2
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• pp.225-231
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• 2015

This study was conducted to examine the physicochemical properties and micro-encapsulation process of rice fermented with Bacillus subtilis CBD2. The viable bacterial cell, pH, and amylase activity of the rice liquid culture were 7.61 log CFU/mL, pH 5.08 and 159.43 units/mL, respectively. The micro-encapsulated rice liquid culture was manufactured via spray drying with different forming agents: i.e., alginic acid 1.0% and chitosan 0.3%, 0.5%, and 1.0%. The moisture contents of the spray-dried powders were approximately 2.90~3.68%. The color of the L and a value decreased whereas that of the b and ${\Delta}E$ value increased. The particle size and outer topology of the spray-dried rice liquid culture were $48.13{\sim}68.48{\mu}m$ and globular, respectively. The water absorption index of the spray-dried powder (2.40~2.65) was lower than that of the freeze-dried powder (2.66). The water solubility index of the spray-dried powder (9.17~10.89%) was higher than that of the freeze-dried powder (7.12%). The in vitro dissolution was measured for five hours in pH 1.2 simulated gastric fluid, and pH 6.8 and pH 7.4 simulated intestinal fluids, using a dissolution tester at $37^{\circ}C$ with 50 rpm agitation. The amylase survival in the fermented rice was 85.93% through the spray-drying and it was very effectively controlled.

• Journal of the Korean Society of Food Science and Nutrition
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• v.38 no.12
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• pp.1699-1706
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• 2009

This study was conducted to investigate the antioxidative effects of chungkukjang fermented using Bacillus subtilis DJI (DJI CJ) in rats fed high cholesterol diet. Sprague-Dawley male rats weighing 185-195 g were divided into 6 groups: normal group (N), high cholesterol group (C), high cholesterol and DJI CJ with no salt group (C-CJN), high cholesterol and DJI CJ added with solar salt group (C-CJS), high cholesterol and DJI CJ added with refined salt group (C-CJR), and high cholesterol and commercial CJ group (C-CCJ). The body weight gain and food intake in all four CJ groups were lower than C group. The serum activities of AST and ALT that were elevated by high cholesterol diet were significantly decreased by CJ supplemented. The hepatic activities of catalase and SOD in C group were increased to 20.59% and 18.72%, respectively, compared with N group, but those of C-CJN, C-CJS, C-CJR, and C-CCJ groups were similar to those of N group. Liver TBARS contents were significantly decreased in all CJ groups, compared with C group. The contents of brain lipofuscin in C-CJN, C-CJS, C-CJR, and C-CCJ groups were remarkably inhibited about 20.86%, 22.06%, 14.73%, and 12.88%, respectively, compared with C group. There were no significant differences among DJI CJ groups in antioxidative effects. According to this study, DJI chungkukjang or commercial chungkukjang seems to protect tissues from oxidative stress by stimulating antioxidative systems in rats fed a high cholesterol diet.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.1001-1007
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• 1994

In order to develop a natural food preservative, dried salviae miltiorrhizae radix (Salvia miltiorrhiza) was extracted with several solvents, and then antimicrobial activity was investigated. The optimum extracting condition for the antimicrobial sustance from the sample, minimal inhibitory concentration (MIC) of the extracted substance against microorganisms were also examined. Antimicrobial activity of the initial ethanol extract from the sample was the strongest compared to those of other solvent extracts such as n-hexane, acetone, butanol, methanol and water. the optimum extractingcondition for antimicrobial substance from the sample was shaking extraction for 2 hours at room temperature incase that 10 volumes of absolute ethanol was added to crushed Saliva Miltiorrhiza. The ethanol extract had strong growth inhibition activity against Gram-positive Bacteria (MIC, 3.13-50$\mu\textrm{g}$/ml) such as B. cereus, B, subtilis, L. minocytogenes, S. aureus, Sc. Mutans. Among Grampositive bacteria tested, Bacillus species was the most susceptibile to the extracted substance. The antimicrobial activity of the ethanol extract from the sample was weak to Gram -negative bacteria yeasts, for example MIC for Gram-negative bacteria and yeasts was 0.8mg/ml and 0.4-0.8mg/ml , respectively.

• KSBB Journal
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• v.19 no.4
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• pp.291-294
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• 2004

The aim of this study was to figure out the antibacterial pattern of leucocin A transformed yeast with culture. Dry cell weight, total secreted protein, and antibacterial activity were increased to 12 hour, after then they showed decrease while protease activity represented the opposite pattern. This implied the production of leucocin A was growth-related. Compared to the result of one hour culture broth, antibacterial activity was about 3.24 fold at 12 hour culture. Maximum growth inhibition rate was 70.57% compared to nontransformed yeast. As the increase of protease in the supernatant, the antibacterial activity was diminished. This study could permit the mass production of bacteriocin to use as antibiotics or food preservatives.

• Preventive Nutrition and Food Science
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• v.14 no.1
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• pp.90-93
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• 2009

Cheonggukjang was prepared from soybean inoculated with B. licheniformis ATCC 10716 cells transformed with pHY3-5 carrying a fibrinolytic enzyme gene. During the 54 hr of fermentation at $37^{\circ}C$, fibrinolytic activities of cheonggukjang were significantly higher than cheonggukjang fermented with B. licheniformis 10716 control cells. The plasmid, pHY3-5 was stably maintained during the 54 hr without antibiotic selection and more than 52% of cells retained the plasmid.

• Journal of Microbiology and Biotechnology
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• v.24 no.8
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• pp.1073-1080
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• 2014

A total of 10 cellulase-producing bacteria were isolated from soil samples irrigated with paper and pulp mill effluents. The sequencing of 16S rRNA gene revealed that all isolates belonged to different species of genus Bacillus. Among the different isolates, B. subtilis IARI-SP-1 exhibited a high degree of ${\beta}$-1,4-endoglucanase (2.5 IU/ml), ${\beta}$-1,4-exoglucanase (0.8 IU/ml), and ${\beta}$-glucosidase (0.084 IU/ml) activity, followed by B. amyloliquefaciens IARI-SP-2. CMC was found to be the best carbon source for production of endo/exoglucanase and ${\beta}$-glucosidase. The ${\beta}$-1,4-endoglucanase gene was amplified from all isolates and their deduced amino acid sequences belonged to glycosyl hydrolase family 5. Among the domains of different isolates, the catalytic domains exhibited the highest homology of 93.7%, whereas the regions of signal, leader, linker, and carbohydrate-binding domain indicated low homology (73-74%). These variations in sequence homology are significant and could contribute to the structure and function of the enzyme.

• Journal of Microbiology and Biotechnology
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• v.8 no.1
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• pp.28-33
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• 1998

A gene coding for ${\beta}$-xylosidase from thermophilic xylanolytic Bacillus sp. KK-1 was cloned into Escherichia coli using plasmid pBR322. Recombinant plasmid DNAs were isloated from E. coli clones which were capable of hydrolyzing 4-methylumbelliferyl-${\beta}$-D xylopyranoside. Restriction analysis showed the DNAs to share a common insert DNA. Xylo-oligosaccharides, including xylotriose, xylotetraose, xylopentaose, and xylobiose were hydrolyzed to form xylose as an end product by cell-free extracts of the E. coli clones, confirming that the cloned gene from strain KK-1 is ${\beta}$-xylosidase gene. The ${\beta}$-xylosidase gene of strain KK-1 designated as xylB was completely sequenced. The xylB gene consisted of an open reading frame of 1,602 nucleotides encoding a polypeptide of 533 amino acid residues, and a TGA stop codon. The 3' flanking region contained one stem-loop structure which may be involved in transcriptional termination. The deduced amino acid sequence of the KK-1 ${\beta}$-xylosidase was highly homologous to the ${\beta}$-xylosidases of Bacillus subtilis and Bacillus pumilus, but it showed no similarity to a thermostable ${\beta}$-xylosidase from Bacillus stearothermophilus.

• Journal of Microbiology and Biotechnology
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• v.3 no.3
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• pp.139-145
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• 1993

The nucleotide sequence of the xylanase gene (xynS) from alkali-tolerant Bacillus sp. YA.14 was determined and analyzed. A 639 base pairs open reading frame for xynS gene was observed and encoded for a protein of 213 amino acids with a molecular weight of 23, 339. S1 nuclease mapping showed that the transcription initiation site of the xynS gene did not exist in the cloned DNA. Ribosome binding site sequence with the free energy of -18.8 Kcal/mol was observed 8 base pairs upstream from the initiation codon, ATG. The proposed signal sequence consisted of 28 amino acids, of which 3 were basic amino acid residues and 21 were hydrophobic amino acid residues. When the amino acid sequences of xylanases were compared, Bacillus sp. YA-14 xylanase showed 48% homology with Bacillus sp. YC-335 xylanase and 96% homology with xylanases from B. subtilis and B. circulans.

• Journal of Microbiology and Biotechnology
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• v.21 no.5
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• pp.515-518
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• 2011

A gene encoding bacillopeptidase F, bpr86-1, was cloned from B. amyloliquefaciens CH86-1 isolated from cheonggukjang. This gene could encode a preproenzyme of 1,431 amino acids. When bpr86-1 was introduced into B. subtilis WB600 via pHY300PLK, an E. coli-Bacillus shuttle vector, the transformant showed fibrinolytic activity. During growth on LB, the fibrinolytic activity of cells increased sharply when they entered the stationary phase. The highest activity (761.4 mU/mg protein) was observed at 96 h of cultivation.

• BMB Reports
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• v.44 no.3
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• pp.193-198
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• 2011

The chitinase-producing strain SC081 was isolated from Korean traditional soy sauce and identified as Bacillus atrophaeus based on a phylogenetic analysis of the 16S rDNA sequence and a phenotypic analysis. A gene encoding chitinase from B. atrophaeus SC081 was cloned in Escherichia coli and was named SCChi-1 (GQ360078). The SCChi-1 nucleotide sequences were composed of 1788 base pairs and 596 amino acids, which were 92.6, 89.6, 89.3, and 78.9% identical to those of Bacillus subtilis (ABG57262), Bacillus pumilus (ABI15082), Bacillus amyloliquefaciens (ABO15008), and Bacillus licheniformis (ACF40833), respectively. A recombinant SCChi-1 containing a hexahistidine tag at the amino-terminus was constructed, overexpressed, and purified in E. coli to characterize SCChi-1. $H_6SCChi$-1 revealed a hydrolytic band on zymograms containing 0.1% glycol chitin and showed the highest lytic activity on colloidal chitin and acidic chitosan. The optimal temperature and pH for chitinolytic activity were $50^{\circ}C$ and pH 8.0, respectively.