• Food Science and Biotechnology
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• v.16 no.6
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• pp.1069-1071
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• 2007

The frequency independent critical concentration (Cc) of xanthan and carob (X/C) mixed gel was determined based on the Winter-Chambon's theory. X/C mixed (X/C=1:1 ratio) gels were prepared from 0.1 to 1% of concentration. The linear viscoelastic properties, i.e., storage and loss modulus, of X/C mixed gel at $20^{\circ}C$ were measured by frequency sweep tests. The frequency independence of tangent function of phase angle (tan ${\delta}$) of X/C mixed gels was graphically determined from the intersection of the plot of phase angle against concentration at varied frequencies. The intersection (C=0.43%) was considered to be Cc of X/C mixed gel.

• Korean Journal of Microbiology
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• v.52 no.3
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• pp.336-343
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• 2016

A mannanase gene was cloned into Escherichia coli from Cellulosimicrobium sp. YB-43, which had been found to produce two kinds of mannanase, and sequenced completely. This mannanase gene, designated manB, consisted of 1,284 nucleotides encoding a polypeptide of 427 amino acid residues. Based on the deduced amino acid sequence, the ManB was identified to be a modular enzyme including two carbohydrate binding domains besides the catalytic domain, which was highly homologous to mannanases belonging to the glycosyl hydrolase family 5. The N-terminal amino acid sequence of ManB, purified from a cell-free extract of the recombinant E. coli carrying a Cellulosimicrobium sp. YB-43 manB gene, has been determined as QGASAASDG, which was correctly corresponding to signal peptide predicted by SignalP4.1 server for Gram-negative bacteria. The purified ManB had a pH optimum for its activity at pH 6.5~7.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum (LBG), konjac and guar gum, while it did not exhibit activity towards carboxymethylcellulose, xylan, starch, and para-nitrophenyl-${\beta}$-mannopyranoside. The activity of enzyme was inhibited very slightly by $Mg^{2+}$, $K^+$, and $Na^+$, and significantly inhibited by $Cu^{2+}$, $Zn^{2+}$, $Mn^{2+}$, and SDS. The enzyme could hydrolyze mannooligosaccharides larger than mannobiose, which was the most predominant product resulting from the ManB hydrolysis for mannooligosaccharides and LBG.

• Journal of Life Science
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• v.27 no.9
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• pp.1003-1010
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• 2017

An open reading frame coding for mannanase predicted from the partial genomic sequence of Paenibacillus woosongensis was cloned into Escherichia coli by polymerase chain reaction amplification, and completely sequenced. This mannanase gene, designated man26AT, consisted of 3,162 nucleotides encoding a polypeptide of 1,053 amino acid residues. Based on the deduced amino acid sequence, Man26AT was identified as a modular enzyme, which included a catalytic domain belonging to the glycosyl hydrolase family 26 and two carbohydrate-binding modules, CBM27 and CBM11. The amino acid sequence of Man26AT was homologous to that of several putative mannanases, with identity of 81% for P. ihumii and identity of less than 57% for other strains of Paenibacillus. A cell-free extract of recombinant E. coli carrying the man26AT gene showed maximal mannanase activity at $55^{\circ}C$ and pH 5.5. The enzyme retained above 80% of maximal activity after preincubation for 1 h at $50^{\circ}C$. Man26AT was comparably active on locust bean gum (LBG), galactomanan, and kojac glucomannan, whereas it did not exhibit activity on carboxymethylcellulose, xylan, or para-nitrophenyl-${\beta}$-mannopyranoside. The common end products liberated from mannooligosaccharides, including mannotriose, mannotetraose, mannopentaose, and mannohexaose, or LBG by Man26AT were mannose, mannobiose, and mannotriose. Mannooligosacchrides larger than mannotriose were found in enzymatic hydrolyzates of LBG and guar gum, respectively. However, Man26AT was unable to hydrolyze mannobiose. Man26AT was intracellularly degraded into at least three active proteins with different molecular masses by zymogram.

• Korean Journal of Microbiology
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• v.54 no.2
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• pp.126-135
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• 2018

The characteristics of enzyme and gene for mannanase B had been reported from Cellulosimicrobium sp. YB-43 producing some kind of mannanase. A gene coding for the enzyme, named mannanase C (ManC), was expected to be located downstream of the manB gene. The manC gene was cloned by polymerase chain reaction and sequenced completely. From this nucleotide sequence, ManC was identified to consist of 448 amino residues and contain a carbohydrate binding domain CBM2 besides a catalytic domain, which was homologous to mannanase belonging to the glycosyl hydrolase family 5. The catalytic domain of ManC showed the highest amino acid sequence similarity of 55% with the mannanases from Streptomyces sp. SirexAA-E (55.8%; 4FK9_A) and S. thermoluteus (57.6%; BAM62868). The His-tagged ManC (HtManC) lacking N-terminal signal peptide with hexahistidine at C-terminus was produced and purified from cell extract of recombinant Escherichia coli. The purified HtManC showed maximal activity at $65^{\circ}C$ and pH 7.5, with no significant change in its activity at pH range from 7.5 to 10. HtManC showed more active on konjac and locust bean gum (LBG) than guar gum and ivory nut mannan (ivory nut). Vmax and Km values of the HtManC for LBG were 68 U/mg and 0.45 mg/ml on the optimal condition, respectively. Mannobiose and mannotriose were observed on TLC as major products resulting from the HtManC hydrolysis of mannooligosacharides. In addition, mannobiose and mannose were commonly detected as the hydrolyzed products of LBG, konjac and ivory nut.

• Microbiology and Biotechnology Letters
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• v.32 no.4
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• pp.347-351
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• 2004

Hydrolysis of manno-oligosaccharides and galactomannan was studied with the purified Bacillus subtilis WL-7 mannanase from recombinant Eschericoli. The predominant products of hydrolysis were mannose, mannobiose and mannotriose. The enzyme could hydrolyze $\beta$-1 A-linked manno-oligosaccharides larger than mannobiose, but was not active on mannobiose. When the mannanase hydrolyzed manno-oligo saccharides of degree of polymerization(DP) 4-6, it was more active on the substrate of higher DP. Based on analysis of transient reaction products by TLC, the enzyme was found to have a preference for internal $\beta$-IA-mannosidic linkages, which are the central mannosidic bond of mannotetraose and the two middle mannosidic bonds of mannopentaose. The $\beta$-l A-mannosidic bonds situated at the second and fourth positions from the nonreducing end of mannohexaose were preferenhydrolyzed by the mannanase. Locust bean gum(LBG) was enzymatically hydrolyzed with higher efficiency than guar gum, resulting that amount of reducing sugars was liberated more efficiently from LBG than guar gum with same activity of mannanase.

• Food Engineering Progress
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• v.13 no.4
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• pp.320-325
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• 2009

The effects of adding additives such as vital gluten, gum, emulsifier, and enzyme to rice flour on baking quality were examined. The effects of different gums on the pasting and dough properties of rice flour containing vital gluten were studied using a Rapid Visco Analyzer (RVA) and a Brabender farinograph. The RVA peak, breakdown, and final viscosities decreased with the addition of gums, while setback viscosity increased. The farinogram showed that rice flour supplemented with gums such as tara gum, guar gum, and locust bean gum (LBG) increased water absorption and dough stability, yielding strengthened dough similar to wheat flour dough. The addition of guar or tara gum/sodium stearoyl lactylate (SSL)/fungal $\alpha$-amylase (AMYL) or glucose oxidase (GO) blend improved the volume and reduced the crumb firmness of rice bread prepared from rice flour containing 14% vital gluten. Therefore, the combined addition of gum, emulsifier and enzyme into rice flour significantly improved the rice bread quality, allowing the decrease of the vital gluten level in rice bread formula.

• Korean Journal of Soil Science and Fertilizer
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• v.38 no.5
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• pp.287-293
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• 2005

In this work, to develop soil inoculant which maintains stable viable cells and normalized quality, studies on micro-encapsulation with bacteria and yeast cells were performed by investigating materials and methods for micro-encapsulation as well as variation and stability of encapsulated cells. Preparation of capsule was conducted by application of extrusion system using micro-nozzle and peristaltic pump. K-carragenan and Na-alginate were selected as best carrier for gelation among K-carageenan, Na-alginate, locust bean gum, cellulose acetate phthalate (CAP), chitosan and gelatin tested. Comparing the gels prepared with Bacillus sp. KSIA-9 and carriers of 1.5% concentration, although viable cell of K-carragenan and Na-alginate was six times higher than those of other, Na-alginate was finally selected as carrier for gelation because it is seven times cheaper than K-carragenan. The gel of 1.5% Na-alginate was also observed to have the best morphology with circular hardness polymatrix and highest viable cell. When investigating the stability of encapsulated cells and the stabilizer effect, free cells were almost dead within 30 or 40 days whereas encapsulated cells decreased in 10% after 30 days and 15-30% even after 120 days. As stabilizer for maintaining viable cell, both 1% starch and zeolite appeared to possess the level of 70-80% cell for bacteria and yeast until after 120 days.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1295-1302
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• 2004

A gene encoding the mannanase of Bacillus subtilis WL-7, which had been isolated from Korean soybean paste, was cloned into Escherichia coli, and the gene product was purified from the culture filtrate of the recombinant E. coli. This mannanase gene, designated manA, consisted of 1,086 nucleotides, encoding a polypeptide of 362 amino acid residues. The deduced amino acid sequence was highly homologous to those of mannanases belonging to the glycosyl hydrolase family 26. The molecular mass of the purified mannanase was 38 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum at 6.0 and a temperature optimum at $55^{\circ}C$. The enzyme was active on locust bean gum, konjak, guar gum, and lichenan, while it did not exhibit activity towards yeast mannan, laminarin, carboxymethylcellulose, $\beta$­glucan, xylan, and para-nitrophenyl-$\beta$-mannopyranoside.

• Journal of Microbiology and Biotechnology
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• v.19 no.10
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• pp.1184-1190
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• 2009

A thermostable extracellular $\beta$-mannanase from the culture supernatant of a fungus Aspergillus niger gr was purified to homogeneity. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 66 kDa. The $\beta$-mannanase exhibited optimum catalytic activity at pH 5.5 and $55^{\circ}C$. It was thermostable at $55^{\circ}C$, and retained 50% activity after 6 h at $55^{\circ}C$. The enzyme was stable at a pH range of 3.0 to 7.0. The metal ions $Hg^{2+}$, $Cu^{2+}$, and $Ag^{2+}$ inhibited complete enzyme activity. The inhibitors tested, EDTA, PMSF, and 1,10-phenanthroline, did not inhibit the enzyme activity. N-Bromosuccinimide completely inhibited enzyme activity. The relative substrate specificity of enzyme towards the various mannans is in the order of locust bean gum>guar gum>copra mannan, with $K_m$ of 0.11, 0.28, and 0.33 mg/ml, respectively. Since the enzyme is active over a wide range of pH and temperature, it could find potential use in the food-processing industry.

• Korean journal of food and cookery science
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• v.12 no.1
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• pp.20-26
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• 1996

The present study was attempted to investigate and to evaluate various hydrocolloids as a stabilizer in improving texture of the frozen yogurt. Four kinds of hydrocolloids used in this study were CMC (carboxymethyll cellulose), PGA(propylene glycol alginate), LMP(low methoxyl pectin), and the combination of LBG(locust bean gum) and GG(guar gum). The viscosity of frozen yogurt mixes did not show any significant differences among four samples at 5$^{\circ}C$. However, as the temperature increased up to 50$^{\circ}C$, theviscosity of frozen yogurt mixes containing CMC, LMP, PGA decreased drastically except frozen yogurt containing the combination of LBG+GG. The overrun of frozen yogurt containing each hydrocolloid gradually increased and reached to about 53, 50, 54, and 35%, respectively, after 40 min of operating ice cream freezer. As the result of sensory evaluation in the texture of frozen yogurt and melt-down quality, the sample containing LMP was described as the most coarce & icy, crumbly, and sand-like characters. On the other hand, PGA sample was evaluated as not being icy, crumbly, but being chewy and soft in texture. However, any significant differences among four samples were not shown in melt-down quality.