• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.4
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• pp.563-569
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• 2013

This study was carried out to investigate the dose-response of chitooligosaccharide (with a molecular weight of 1~3 kDa) on antimicrobial activity and lipid lowering functions in rats. Sprague-Dawley male rats were given experimental diets containing 0 (control), 0.5, 2, or 5% chitooligosaccharide (COS) for 5 weeks. Weight gain and food intake were significantly lower in rats fed 5% COS than control rats and rats fed 0.5 and 2% COS. The numbers of fecal bacteria, including bifidobacteria, lactobacilli, bacteroides, total anaerobes, and total aerobes, which reflect gut microbiota, were significantly decreased in rats fed 5% COS. Plasma triglyceride concentrations significantly decreased in a dose-dependent manner in rats fed 2% or 5% COS, while plasma total cholesterol was not significantly different among groups. The hepatic concentration of triglycerides was lower in rats fed 5% COS, and fecal triglycerides significantly increased in rats fed 5% COS. These results indicate that 5% COS supplementation in a diet may exert antimicrobial activity in vivo, and inhibit the proliferation of typical gut microbes, while lowering lipids.

• Proceedings of the Korean Journal of Food and Nutrition Conference
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• 2002.06a
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• pp.37-37
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• 2002

• Horticultural Science & Technology
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• v.33 no.3
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• pp.383-389
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• 2015

Chitooligosaccharide (COS), as antioxidant, extensively applied to food and juice preservation. In the present study, influences of COS on vase life and ornamental value of cut roses were investigated. Results showed that vase life of cut roses treated by COS was longer 6.4 days than one of control and ornamental character of cut roses was improved effectively by COS. The increase of vase life and ornamental value were chiefly governed by that COS improved water absorption capacity of cut roses. Besides that, COS decreased the contents of superoxide anion and hydrogen peroxide and lowered the levels of malondialdehyde in turn during the senescence process of cut roses. That was because that COS not only enhanced activities of antioxidant enzymes glutathione reductase, but also improved reduced glutathione contents in petals of cut rose. Therefore, COS could be used in commercial preservatives to improve the longevity of cut roses.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2002.04a
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• pp.27-28
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• 2002

• Proceedings of the Korean Fiber Society Conference
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• 1999.10a
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• pp.53-56
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• 1999

• Journal of the East Asian Society of Dietary Life
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• v.25 no.3
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• pp.513-524
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• 2015

The effects of four different oligosaccharides with 2, 4, 6% (w/w) (fructo-oligosaccharide, xylo-oligosaccharide, chito-oligosaccharide and soybean-oligosaccharide) on gelatinization and retrogradation of sulgidduks (Korean rice cake) were examined. The amylograph results of rice flour showed that chito-oligosaccharide hastened gelatinization, and delayed retrogradation. Blue value results of chito-oligosaccharide added sulgidduks showed retarded retrogradation during storage (1, 2 and 3 days). Chitooligosaccharide and xylo-oligosaccharide added sulgidduks showed significantly lower hardness during storage. Lightness (L) decreased and redness (a) and yellowness (b) increased with increasing oligosaccharide amounts. In the sensory evaluation of sulgidduks, color of fructo-oligosaccharide added sulgidduks obtained the highest score among oligosaccharide added sulgidduks. During storage, xylo-oligosaccharide and fructo-oligosaccharide added sulgidduks had higher flavor, taste, graininess and overall quality scores than the control. Physicochemical tests showed that chito-oligosaccharide retarded retrogradation, whereas chitooligosaccharide- added sulgidduks had low scores in sensory tests due to aftertaste of chito-oligosaccharide. To improve the sensory quality of chito-oligosaccharide added sulgidduks, mixtures of chito-oligosaccharide with xylo-oligosaccharide and fructooligosaccharide were applied at ratios of 3%:3%, 2%:4% and 1%:5%, respectively. The addition of chito-oligosaccharide and xylo-oligosaccharide at ratios of 2%:4% and 1%:5% to sulgidduks showed relatively high scores in the sensory evaluation retarding retrogradation.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.563-566
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• 2000

In order to obtain microbial endochitosanase for enzymatic production of chitooligosaccharides from chitosan, we screened four microbes from soil and selected. Bacillus sp. HSB-21 which showed highest activity. Chitosanase, produced from isolating microbe, was endo-type and molecular mass of the enzyme was estimated as 21,000 by active staining. Its optimum pH and temperature were 5.5 and $50^{\circ}C$, respectively. It was stable in the pH range of 3.0 to 8.0 and up to $40^{\circ}C$. It did not produce chitomonosaccharide and produced chitooligosaccharide ranging from chitobiose to chitooctaose as major end-products from chitosan. The chitosanase from Bacillus sp. HSB-21 can be applicable to enzymatic production of chitooligosaccharide which has high degree of polymerization .

• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.567-573
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• 1996

Chitinase (EC 3.2.1.14) from culture fluid of Bacillus licheniformis KFB-C14 was purified 66-folds to homogenity in overall yield of 21% by ammonium sulfate fractionation, DEAE-Toyopearl, Butyl-Toyopearl and TSK-Gel HW-55F column chromatography. The enzyme protein had a molecular weight of about 86,000 and was composed of one subunit. The enzyme was significantly stable not only at high temperature but also on treatment with organic solvents and protein denaturants such as SDS, urea and guanidine-HC1. The optimum temperature and pH for reaction was 60$\circ $C and 6.0, respectively. The enzyme activity was inhibited by only Mn$^{2+}$ ion, but not inhibited by EDTA, N- ethylmaleimide and pCMB. The enzyme had high activity with colloidal chitin (V$_{max}$: 421) and commercial chitin (V$_{max}$: 480), but not with typical substrates of exo type chitinase. The thermostable chitinase had an useful reactivity for producing functional chitooligosaccharide, showing the production of (GlcNAc)$_{1}, (GlcNAc)$_{3}$, and (GlcNAc)$_{2}$ as major product.

• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.560-566
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• 1996

A strain capable of producing thermostable chitinase suitable for chitooligosaccharide production was isolated from high temperature environment and identified as Bacillus licheniformis. The chitinase from Bacillus licheniformis KFB-Cl4 was only induced by addition of colloidal thitin into the basal medium as carbon source, showing the decrease of the chitinase production by supplernental addition of other carbon sources into the medium containing 1.0% colloidal chitin. Among organic and inorganic nitrogen sources, yeast extract was the most effective for the increase of total activity and specific activity, and had high affinity for the enzyme production. The optimum temperature of cell growth and thermostable chitinase production was 55$\circ$C. The optimum culture medium was composed of 1.2% colloidal chitin, 0.15% K$_{2}$HPO$_{4}$, 0.05% KH$_{2}$PO$_{4}$, 0.01% MgSO$_{4}$-7H$_{2}$O, 0.1% yeast extract (pH 6.5). Bacillus licheniformis KFB-C14 produced the thermostable chitinase of 3.89 units per ml culture fluid and 7.4 units per mg protein under rotary shaking at 150 rpm for 40 hr.

• Applied Biological Chemistry
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• v.37 no.1
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• pp.43-48
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• 1994

A basic inducible protein, ICG, containing chitinase and ${\beta}-1,3-glucanase$ activity concomittantly was purified from cell suspension culture media of rice after the treatment of chitooligosaccharides. The isolated ICG enzyme gave a single band on native and SDS polyacrylamide gel electrophoresis and its molecular weight was estimated to be 52.53 kd. The optimal temperature and optimal pH of both enzyme activities in ICG were $60^{\circ}C$, pH 6.0 for chitinase activity and $37^{\circ}C$, pH 4.0 for ${\beta}-1,3-glucanase$ activity. $K_M$ and $V_{max}$ values for chitinase were 0.474 mM. 2.997 nM/min., and those for ${\beta}-1,3-glucanase$ were 1.004 mM 0.739 nM/min. respectively. TLC analysis of the chitooligosaccharide hydrolysates with ICG enzyme indicated that ICG acts as endochitinase.