• Korean Journal of Food Science and Technology
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• v.46 no.2
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• pp.121-126
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• 2014

Recently, infant formula products made of caprine milk have gained popularity, mainly because the nutritional composition of caprine milk is similar to that of human milk. In addition, caprine milk is considered to be better than bovine milk in terms of nutrient composition and easier digestion. Compared to bovine milk, caprine milk contains more ${\beta}$-casein, but less ${\alpha}$S1-casein. While the lactose concentration of both bovine and caprine milk is almost the same, a content of total oligosaccharides in caprine milk was approximately five to eight times higher than that in bovine milk. However, as the dairy goat industry in Korea is in a nascent stage of milk production and further processing, many nutritional advantages of caprine milk over bovine milk are not fully conveyed to general consumers. It is recommended that scientific research regarding the nutritional benefits of caprine milk needs to be conducted urgently, owing to the increasing domestic sales of infant formula products made of caprine milk.

• Microbiology and Biotechnology Letters
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• v.20 no.5
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• pp.574-582
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• 1992

Exo-xylanase encoded by the xylA gene of Bacillus stearothermoPhillus was produced from Escherichia coli ]M109 carrying a recombinant plasmid pMGL Synthesis of the enzyme was observed to be cell-associated, and about 94% of the enzyme synthesized was located in the cytoplasmic region. The maximum production was attained when the E. coli strain was grown at $37^{\circ}C$ for 8 hours on the medium containing 0.5% fructose, 1.0% tryptone, 1.0% sodium chloride, and 0.5% yeast extract. The exo-xylanase was purified to homogeneity using a combination of salting out with ammonium sulfate, DEAE-Sepharose CL-6B ion exchange chromatography, Sephadex G-IOO gel filtration, and Sephadex G-150 gel filtration. The' purified enzyme was most active at pH 6.0 and $45^{\circ}C$. $Ca^{2+}$ and $Co^{2+}$ activated the exo-xylanase activity by about 20% while $Ag^{2+}$, $Fe^{2+}$, $Mg^{2+}$ and $Zn^{2+}$ inhibited the enzyme activity by up to 60%. The $K_m$, value on p-nitrophenyl-$\beta$-D-xylanopyranoside was 2.75 mM. The enzyme had a pI value of 4.7. The estimated molecular weight of the native protein was 200,000 daL SDS-polyacrylamide gel electrophoresis analysis suggested that the native enzyme was a trimer composed of three identical 66,000 da!. polypeptides. The purified enzyme efficiently converted all the xylo-oligosaccharides tested to xylose. It was also confirmed that the enzyme split xylans in an exo-manner even though the degree of hydrolysis was fairly low. The xylanolytic enzyme was, therefore, classified to be one of the few bacterial exo-xylanases lacking transferase activity.

• The Korean Journal of Food And Nutrition
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• v.28 no.6
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• pp.1026-1032
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• 2015

This study attempted to find an efficient method for the preparation of high-purity galactooligosaccharides (HP-GOS) using ${\beta}$-galactosidase and yeast fermentation. GOS prepared using Lactozym 3000L showed the greatest enhancement in total GOS of the six ${\beta}$-galatosidases tested. GOS alone achieved 51% conversion of initial lactose. GOS production was enhanced by fermentation with commercial yeast (Saccharomyces cerevisiae); its concentration reached 71% after 36h fermentation with 8% yeast. Component sugar analysis with HPLC indicated that HP-GOS fermented with S. cerevisiae showed significantly increased levels of 4'/6'-galactosyllactose and total GOS as well as a significantly decreased glucose level. HP-GOS facilitated the growth of Lactobacillus sp. (L. acidophilus and L. casei) and Bifidobacterium sp. (B. longum and B. bifidum). In sum, high-purity GOS has been successfully produced through both an enzymatic process and yeast fermentation. GOS encourages the growth of bacteria such as Lactobacillus and Bifidobacterium that may be beneficial to human gastrointestinal health.

• KSBB Journal
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• v.13 no.2
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• pp.147-154
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• 1998

Enzymatic hydrolysis using an immobilized enzyme was carried out to produce chitosan oligosaccharides (COSs) from chitosan effectively. Chitosanase was immobilized on eight different carriers by physical adsorption. The enzyme immobilized on chitin had higher activity than those immobilized on the other carriers in spite of its lower adsorption. The activity of chitin-immobilized enzyme was more than 90% of the original activity. Optimal temperature of the immobilized enzyme increased by about $15^{\circ}C$ and its thermostability was excellent in relatively wide range of temperature. But its effects of pH did not improve compared to the free enzyme. The immobilized enzyme produced 153 mg/g chitosan of the reducing sugar for 3hrs of hydrolytic incubation time. The total content of higher oligomers, tetramer to hexamer, among amount of total COSs obtained for 2hrs was more than 90%. In kinetic parameters for both enzymes, immobilized enzyme showed lower affinity for substrate and reaction rate than free enzyme, however, no reduction of the rate for high substrate concentrations. Consequently, chitin-immobilized could effectively hydrolyse chitosan and produce the higher COSs without activity decrease in comparison with the free enzyme.

• Korean Journal of Microbiology
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• v.42 no.2
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• pp.142-148
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• 2006

In order to develop chitosanase for the production of chitosan oligosaccharides, a chitosanase-producing bacterium was isolated from the traditional fermented soybean, Meju, and identified as Bacillus amyloliquefaciene MJ-1. The cloned chitosanase gene, 825 bp in size, encoded a single peptide of 274 amino acids with a estimated molecular mass of 30.9 kDa. The deduced amino acid sequence showed significant homology with microbial chitosanases. The recombinant chitosanase was expressed in Escherichia coli upon induction with isopropyl-D-thiogalactopyranoside, and purified using $Ni^{2+}-NTA$ agarose column chromatography. The maximal activity of the recombinant chitosanase is at pH 5.0 and $60^{\circ}C$. The recombinant chitosanase is stable between pH 5.0 and pH 7.0 at $37^{\circ}C$ for 30 min, and more than 75% of the activity still remain at $80^{\circ}C$ for 30 min incubation.

• Journal of Life Science
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• v.15 no.6 s.73
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• pp.884-888
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• 2005

An agar-degrading bacterium was isolated from north-eastern sea of Jeju island and cultured in marine agar 2216 media. Biochemical and morphologicl characteristics and 165 rRNA gene revealed that isolated strain was member of Agarivorans genus, and named Agarivorans sp. JA-1. Agarase was produced as growth-related and expressed regardless of agar presence. Optimal pH was 8 at 50 mM Clycine-NaOH buffer, and activity was maximum at $40^{\circ}C$E Enzymatic activity was maintained over $80\%$ at $60^{\circ}C$t and $70\%$ at $80^{\circ}C$ which is thermotolerant. Hence isolated novel Agarivorans sp. JA-1 strain and its beta-agarase could be used for the production of functional oligosaccharide from agar in solution state.

• Food Engineering Progress
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• v.14 no.4
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• pp.359-366
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• 2010

Large-scale preparation steps of antithrombotic materials from wood ear mushroom (Auricularia auricular-judae) were established as follows. Grounded dry wood ear mushroom was extracted with 75% ethanol and its precipitate was extracted with $76^{\circ}C$ water for 2 hr followed by filter pressing. The filtrate was then concentrated by vacuum and extracted with 80% ethanol, and the resulting precipitate was then freeze-dried. The formula of the product was determined using consumer susceptibility tests as follows; mushroom extract 90.5%, high fructose corn syrup 2.0%, $\beta$-cyclodextrin 1.5%, fructo-oligosaccharide 2.0%, pear puree 4.0%. When the packed products were stored at 25, 37, or $45^{\circ}C$ for 8 weeks, there were no noticeable changes in water activity, moisture content, pH, and acidity. The viable cell number of total bacteria was slightly increased during the storage period at 25 and $37^{\circ}C$, The total bacteria were not detected in the product when stored at $45^{\circ}C$. When the product was injected intravenously into rat at the level of 1,000 mg/kg, antithrombotic activities such as activated partial thromboplastin time, thrombin time, prothrombin time, and FIB were increased when compared with the control group. When the product was administrated orally into rat at the level of 500 mg/kg, it showed the same antiplatelet activity to aspirin.

• Microbiology and Biotechnology Letters
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• v.49 no.3
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• pp.329-336
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• 2021

Cellulophga sp. J9-3, is a gram-negative, aerobic marine bacterium belonging to the family Flavobacteriaceae. In addition to cellulose degradability, the J9-3 strain is also capable of hydrolyzing agar in the solid and liquid medium, and the production of agarase in the presence of agarose can be remarkably induced by the bacterium. From the cell culture broth of Cellulophga sp. J9-3, ammonium sulfate precipitation and three kinds of column chromatography were successively performed to purify a specific agarase protein, the AgaJ93. Purified AgaJ93 showed the strongest hydrolyzing activity towards agarose (approximately 22%), and even displayed activity towards starch. AgaJ93 hydrolyzed agarose into neoagarotetraose and neoagarohexaose via various oligosaccharide intermediates, indicating that AgaJ93 is an endo-type β-agarase. AgaJ93 showed maximum activity at a pH of 7.0 and temperature of 35 ℃. Its activity increased by more than six times in the presence of Co²⁺ ions. The N-terminal sequence of AgaJ93 showed 82% homology with the heat-resistant endo-type β-agarase Aga2 of Cellulophaga sp. W5C. However, the biochemical properties of the two enzymes were different. Therefore, AgaJ93 is expected to be a novel agarose, different from the previously reported β-agarases.

• Animal Bioscience
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• v.35 no.12
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• pp.1892-1903
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• 2022

Objective: A series of experiment were conducted to evaluate the effects of replacing a part of soybean meal (SBM) at 6% of broiler diets with fermented soybean meal (FSBM) obtained by single or two-stage fermentation by measuring growth performance, antioxidant activity in the jejunum and distal intestinal microflora. Methods: Soybean meal samples were prepared by single-stage fermentation using Bacillus velezensis (Bv) (FSBM_B), or Lactobacillus spp. (as commercial control) (FSBM_L). Additional SBM sample was prepared by two-stage fermentation using Bv and subsequently using Lactobacillus brevis ATCC 367 (Lb) (FSBM_B+L). Enzyme activity, chemical composition, trichloroethanoic acid-nitrogen solubility index (TCA-NSI) and antioxidant activity were measured. Then, in an in vivo study, 320 Ross308 broilers were divided into four groups with ad libitum supply of feed and water. Four groups were fed either a corn-soybean meal diet (SBM), or one of fermented SBM diets (FSBM_B+L, FSBM_B, and FSBM_L). Growth, serum characteristics, microflora, and the mRNA expression of selected genes were measured. Results: Compared to SBM, FSBM_B+L contained lower galacto-oligosaccharide, allergic protein, and trypsin inhibitor, and higher TCA-NSI by about three times (p<0.05). Reducing power and 1,1-diphenyl-2-picrylhydrazyl free radical scavenging ability correlated positively with the TCA-NSI content in FSBM. Growth performances were not significantly different among four groups. In jejunum of 35-day-old broilers, partial replacement of SBM by FSBM_B+L increased the activity of superoxide dismutase and catalase (CAT), and the FSBM_B group had the highest catalase activity (p<0.05). Partial replacement of SBM by FSBM increased relative mRNA expressions of nuclear factor erythroid 2-related factor 2 (Nrf2), heme oxygenase-1 (HO-1), and peptide transporter 1 (PepT1) (p<0.05); however, FSBM_B+L increased CAT mRNA level to 5 times of the control (p<0.05). Conclusion: Using Bv- and Lb-processed SBM through two-stage fermentation to partially replace 6% of diets will improve the gut's antioxidant activity under commercial breeding in broilers.

• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.3
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• pp.434-440
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• 2013

This study was conducted to screen the characteristics and alginate-degrading activity of marine bacterium isolated from brown seaweed (Sargassum thunbergii). The results of 16S ribosomal RNA sequence analysis the strain the genus Vibrio and the strain was subsequently named Vibrio sp. PKA 1003. The optimum culture conditions for the growth of Vibrio sp. PKA 1003 were at pH 7, 3% NaCl, $25^{\circ}C$, and 6% alginic acid, with a 48-hour incubation time. A crude enzyme preparation from Vibrio sp. PKA 1003, showed its highest levels of alginate-degradation activity when cultured at pH 9, $30^{\circ}C$, and 6% alginic acid, with a 63-hour incubation time. Thin layer chromatography analyses confirmed that the crude enzyme released monomers or oligomers from sodium alginate, and results from trypsin treatment showed that the alginate degrading activity depends on this enzyme produced by Vibrio sp. PKA 1003. These results suggest that Vibrio sp. PKA 1003 and its alginate-degrading crude enzyme is useful for the production of alginate oligosaccharides.