• Food Science of Animal Resources
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• v.33 no.4
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• pp.474-480
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• 2013

This study was performed to investigate the effects of high pressure/high temperature (HPHT) treatment on the recovery efficiency and characteristics of porcine placenta hydrolysates. The placenta hydrolysates were characterized by solubility, free amino acid contents, gel electrophoresis, gel permeation chromatography (GPC) and amino acid composition. Placenta was treated at 37.5 MPa of pressure combined with various temperatures (150, 170, and $200^{\circ}C$) or various holding times (0, 30, and 60 min at $170^{\circ}C$). Insoluble raw placenta collagen was partially solubilized (> 60% solubility) by the HPHT treatment. Free amino group content of placenta collagen was increased from 0.1 mM/g collagen to > 0.3 mM/g collagen after HPHT treatment, reflecting partial hydrolysis of collagen. The molecular weight ($M_w$) distribution showed evidence of collagen hydrolysis by shifting of $M_w$ peaks toward low molecular weight when treated temperature or holding time was increased. Alanine (Ala), glycine (Gly), hydroxyproline (Hyp), and proline (Pro) contents increased after the HPHT treatments compared to a decrease in the others. In particular, the increase in Gly was obvious, followed by Hyp and Pro, reflecting that placenta hydrolysates were mainly composed of these amino acids. However, increasing temperature or holding time hardly affected the amino acid compositions. These results indicate that the HPHT treatment is advantageous to hydrolyze collagen derived from animal by-products.

• Applied Biological Chemistry
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• v.42 no.1
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• pp.6-11
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• 1999

The bacteria which could hydrolyze the fibrin produced through the blood coagulation mechanism in the human body, were isolated from soybean paste. The KDO-13 strain was selected among the isolated bacteria as the best strain for fibrinolytic activity. It was spore forming and Gram positive. $C_{15:0}$ anteiso fatty acid, $C_{15:0}$ iso fatty acid and $C_{15:0}$ anteiso fatty acid were 47.7, 13.5 and 13.6%, respectively as major component among its cellular fatty acid composition. It showed the similarity of 57.7%, compared with standard strain. It was thus identified to be Bacillus atrophaeus according to Bergey's manual of systematic bacteriology and its fatty acid profiles of gas chromatography. The optimum culture temperature and pH were $37^{\circ}$ and 6 for the production of fibrinolytic enzyme by Bacillus atrophaeus KDO-13.

• Journal of Microbiology and Biotechnology
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• v.26 no.2
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• pp.315-325
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• 2016

A novel esterase gene, est7K, was isolated from a compost metagenomic library. The gene encoded a protein of 411 amino acids and the molecular mass of the Est7K was estimated to be 44,969 Da with no signal peptide. Est7K showed the highest identity of 57% to EstA3, which is an esterase from a drinking water metagenome, when compared with the enzymes with reported properties. Est7K had three motifs, SMTK, YSV, and WGG, which correspond to the typical motifs of family VIII esterases, SxxK, Yxx, and WGG, respectively. Est7K did not have the GxSxG motif in most lipolytic enzymes. Three additional motifs, LxxxPGxxW, PLGMxDTxF, and GGxG, were found to be conserved in family VIII enzymes. The results of the phylogenetic analysis and the alignment study suggest that family VIII enzymes could be classified into two subfamilies, VIII.1 and VIII.2. The purified Est7K was optimally active at 40ºC and pH 10.0. It was activated to exhibit a 2.1-fold higher activity by the presence of 30% methanol. It preferred short-length p-nitrophenyl esters, particularly p-nitrophenyl butyrate, and efficiently hydrolyzed glyceryl tributyrate. It did not hydrolyze β-lactamase substrates, tertiary alcohol esters, glyceryl trioleate, fish oil, and olive oil. Est7K preferred an S-enantiomer, such as (S)-methyl-3-hydroxy-2-methylpropionate, as the substrate. The tolerance to methanol and the substrate specificity may provide potential advantage in the use of the enzyme in pharmaceutical and other biotechnological processes.

• Microbiology and Biotechnology Letters
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• v.39 no.3
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• pp.252-258
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• 2011

A bacterial strain capable of hydrolyzing xylan and locust bean gum (LBG) was isolated from farm soil by enrichment culture using mixture of palm kernel meal (PKM) and wheat bran as carbon source. Nucleotide sequence of 16S rDNA amplified from the isolate YB-1107 showed high similarity with those of genus Cellulosimicrobium strains. Xylanase productivity was increased when the Cellulosimicrobium sp. YB-1107 was grown in the presence of wheat bran or oat spelt xylan, while mannanase productivity was increased drastically when grown in the presence of PKM or LBG. Particularly, maximum mannanase and xylanase activities were obtained in the culture filtrate of media containing 0.7% PKM or 1% wheat bran, respectively. Both enzyme activities were produced at stationary growth phase. Mannanase from the culture filtrate showed the highest activity at $55^{\circ}C$ and pH 6.5. Xylanase activity was optimal at $65^{\circ}C$ and pH 5.5. The predominant products resulting from the mannanase or xylanase hydrolysis were oligosaccharides for LBG or xylan, respectively. In addition, the enzymes could hydrolyze wheat bran and rice bran into oligosaccharides.

• Journal of Microbiology and Biotechnology
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• v.20 no.10
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• pp.1378-1385
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• 2010

A novel agarolytic bacterium, KY-YJ-3, producing extracellular agarase, was isolated from the freshwater sediment of the Sincheon River in Daegu, Korea. On the basis of Gram-staining data, morphology, and phylogenetic analysis of the 16S rDNA sequence, the isolate was identified as Cellvibrio sp. By ammonium sulfate precipitation followed by Toyopearl QAE-550C, Toyopearl HW-55F, and MonoQ column chromatographies, the extracellular agarase in the culture fluid could be purified 120.2-fold with a yield of 8.1%. The specific activity of the purified agarase was 84.2 U/mg. The molecular mass of the purified agarase was 70 kDa as determined by dodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature and pH of the purified agarase were $35^{\circ}C$ and pH 7.0, respectively. The purified agarase failed to hydrolyze the other polysaccharide substrates, including carboxymethyl-cellulose, dextran, soluble starch, pectin, and polygalacturonic acid. Kinetic analysis of the agarose hydrolysis catalyzed by the purified agarase using thin-layer chromatography showed that the main products were neoagarobiose, neoagarotetraose, and neoagarohexaose. These results demonstrated that the newly isolated freshwater agarolytic bacterium KY-YJ-3 was a Cellvibrio sp., and could produce an extracellular ${\beta}$-agarase, which hydrolyzed agarose to yield neoagarobiose, neoagarotetraose, and neoagarohexaose as the main products.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.760-763
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• 2001

Five commercial salt-fermented shrimps contained 29.8~48.3% of salt 3.5%~7.3% of total nitrogen and 0.3~0.7g/100g of amino-nitrogen respectively. The average peptide length(APL) of five commercial salt-fermented shrimps ranged from 10.1 to 15.0. Sample B and E showed longer APL than the others with the values of 15.0 and 14.4 respectively. Protease activity showed the large differences in five samples from 17 unit to 232 unit ; sample C showed the highest protease activity with 232 unit while sample D and E were relatively lower with 17 unit and 18 unit respectively. The chitinase activities which can hydrolyze chitin the one of components on outer layer of shrimp ranged from 14.4 unit to 171 unit. Sample E had the highest chitinase activity as 171 unit but sample B showed the lowest activity with 14.4 unit. Chitooligosaccharides of five commercial salted-fermented shrimps were consisted of monoglucosamine diglucosamine and triglucosamine.

• Preventive Nutrition and Food Science
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• v.12 no.4
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• pp.209-216
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• 2007

To investigate the applicability as the functional food materials of germinated Glycine max Merr soybeans, its biochemical characteristics and its abilities to inhibit platelet aggregation and hydrolyze alcohol were examined. With the progression of germination time, crude protein content gradually increased, and on the 5th day of germination it was 30.19%. However, crude fat content tended to decrease, and on the 5th day of germination it was 14.30%. Total amino acid content was highest on the 3rd day of germination at 80,875 mg%. The free amino acid content doubled from day 0 of germination (1,273.35 mg%) until the 5th day of germination (2,742.99 mg%). Fatty acid analysis revealed that linoleic acid was highest among all the samples, ranging from $53.55{\sim}56.00%$. Linolenic acid content slightly increased as the germination period was prolonged. The ability to inhibit platelet aggregation increased according to the germination period and then decreased again on the 5th day of germination; it was somewhat higher in the ethanol fraction. In measuring ADH, we found that the activity of the ethanol fraction increased with increasing days of germination. In the case of the water fraction, the activity decreased as germination was prolonged, and the ADH activity of the water fraction was higher than that of the ethanol fraction. Based on the above results, we deemed that the Glycine max Merr soybeans germinated for $2{\sim}3$ days were most pertinent for use as functional food materials.

• BMB Reports
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• v.37 no.4
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• pp.466-473
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• 2004

A new acid deoxyribonuclease (DNase) was purified from the cultured mycelia of Cordyceps sinensis, and designated CSDNase. CSDNase was purified by $(NH_4)_2SO_4$ precipitation, Sephacryl S-100 HR gel filtration, weak anion-exchange HPLC, and gel filtration HPLC. The protein was single-chained, with an apparent molecular mass of ca. 34 kDa, as revealed by SDS-PAGE, and an isoelectric point of 7.05, as estimated by isoelectric focusing. CSDNase acted on both double-stranded (ds) and single- stranded (ss) DNA, but preferentially on dsDNA. The optimum pH of CSDNase was pH 5.5 and its optimum temperature 55. The activity of CSDNase was not dependent on divalent cations, but its enzymic activity was inhibited by high concentration of the cation: $MgCl_2$ above 150 mM, $MnCl_2$ above 200 mM, $ZnCl_2$ above 150 mM, $CaCl_2$ above 200 mM, NaCl above 300 mM, and KCl above 300 mM. CSDNase was found to hydrolyze DNA, and to generate 3-phosphate and 5-OH termini. These results indicate that the nucleolytic properties of CSDNase are essentially the same as those of other well-characterized acid DNases, and that CSDNase is a member of the acid DNase family. To our knowledge, this is the first report of an acid DNase in a fungus.

• Fashion & Textile Research Journal
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• v.8 no.3
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• pp.343-348
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• 2006

This study aims to attain gray tone dyed goods by using tannin that is contained in green tea. Tannin is given general name of polyphenol, which has a characteristic that bonds with protein and it is used for food preservative that protects against bacteria, as well as its purpose of black tone dye for silk treatment that has been processed since its early ages. In particular, as tannin reacts with all kinds of metallic mordant and changes to various colors, when tannin acid is combined with iron, it becomes tannin steel and produces gray tone color. Tannin that is contained in green tea is condensed tannins and its structure does not hydrolyze, thus having flavan type structure. In order to find the suitable condition for processing tannin, UV-Vis part absorption spectrum of green tea tannin, dye ability based on temperature and time, reflection rate based on concentration, color changes based on acid treatment and alkali treatment, changes on surface based on concentration or metal mordant condition, and lightfastness were measured. Maximum absorption wavelength (${\lambda}_{max}$) of green tea tannin was at around 273nm, while strong absorption was also observed at below 350 nm. Dye ability of green tea tannin is done more easily on silk rather than cellulose fibers such as cotton, while the optimum condition for dyeing was observed to be at $60^{\circ}C$, for 20 minutes. As a result of acid treatment, the color of dye material consisted highly of gray tones and showed overall gray tone with the combined color of yellow and red after the alkali treatment. While it was observed that as dye concentration and metal mordant concentration increased, the color changed at counter-clockwise direction on the Y-scale of Munsell's scale of colors. Additionally, lightfastness was more on a normal fading.

• Journal of Ginseng Research
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• v.36 no.4
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• pp.418-424
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• 2012

This study focused on the enzymatic biotransformation of the major ginsenoside Rb1 into Rd for the mass production of minor ginsenosides using a novel recombinant ${\beta}$-glucosidase from Flavobacterium johnsoniae. The gene (bglF3) consisting of 2,235 bp (744 amino acid residues) was cloned and the recombinant enzyme overexpressed in Escherichia coli BL21(DE3) was characterized. This enzyme could transform ginsenoside Rb1 and gypenoside XVII to the ginsenosides Rd and F2, respectively. The glutathione S-transferase (GST) fused BglF3 was purified with GST-bind agarose resin and characterized. The kinetic parameters for ${\beta}$-glucosidase had apparent $K_m$ values of $0.91{\pm}0.02$ and $2.84{\pm}0.05$ mM and $V_{max}$ values of $5.75{\pm}0.12$ and $0.71{\pm}0.01{\mu}mol{\cdot}min^{-1}{\cdot}mg$ of $protein^{-1}$ against p-nitrophenyl-${\beta}$-D-glucopyranoside and Rb1, respectively. At optimal conditions of pH 6.0 and $37^{\circ}C$, BglF3 could only hydrolyze the outer glucose moiety of ginsenoside Rb1 and gypenoside XVII at the C-20 position of aglycon into ginsenosides Rd and F2, respectively. These results indicate that the recombinant BglF3 could be useful for the mass production of ginsenosides Rd and F2 in the pharmaceutical or cosmetic industry.