• Korean Journal of Food Science and Technology
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• 제22권7호
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• pp.753-761
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• 1990

The physicochemical properties of starches from aerial and subterranean tuber of yam were compared with those of rice and sweet potato. Aerial tuber yam contained higher level of amylose than others, whereas water binding capacity, swelling power and solubility was highest in subterranean tuber yam starch. Brabender amylograms of 5% starch suspensions indicated that the initial pasting temperature of yam starches were slightly higher than that of rice and sweet potato starches, the maximum viscosities of starches from subterranean and aerial tuber yam were 860 and 590 B.U., respectively. Yam starches were more difficult to hydrolyze by ${\alpha}-amylase$ than rice and sweet potato starches. ${\beta}-Amylolysis\;limit$ for yam starches and their amylose and amylopectin were higher than rice and sweet potato starches. The elution profiles of starches on Sepharose CL-2B were different from each other but they were similar between yam starches. Incomplete debranched fractions in the aerial tuber yam amylopectin was particularly higher than other samples. The weight ratio of short chains to long chains for debranched amylopectins was the lowest in aerial tuber yam.

• Korean Chemical Engineering Research
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• 제48권6호
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• pp.704-711
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• 2010

Lignocellulose ($2^{nd}$ generation) is difficult to hydrolyze due to the presence of lignin and the technology developed for cellulose fermentation to ethanol is not yet economically viable. However, recent advances in the extremely new field of biotechnology for the ethanol production are making it possible to use of agriculture residuals and nonedible crops biomass, e.q., rice straw and miscanthus sinensis, because of their several superior aspects as agriculture residual and nonedible crops biomass; low lignin, high contents of carbohydrates. In this article, as the basic study of AP(Ammonia Percolation), the properties and the optium conditions of process were established, and then the overall efficiency of AP was investigated. The important independent variables for AP process were selected as ammonia concentration, reaction temperature, and reaction time. The percolation condition for maximizing the content of cellulose, the enzymatic digestibility, and the lignin removal was optimized using RSM(Response Surface Methodology). The determined optimum condition is ammonia concentration; 11.27%, reaction temperature; $157.75^{\circ}C$, and reaction time; 10.01 min. The satisfying results were obtained under this optimized condition, that is, the results are as follows: cellulose content(relative); 39.98%, lignin content(relative); 8.01%, and enzymatic digestibility; 85.89%.

• Asian-Australasian Journal of Animal Sciences
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• 제30권7호
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• pp.985-993
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• 2017

Objective: The objective of this study was to evaluate increasing doses of a novel microbial phytase (Cibenza Phytaverse, Novus International, St. Charles, MO, USA) on standardized total tract digestibility (STTD) of P in canola meal (CM), corn, corn-derived distiller's dried grains with solubles (DDGS), rice bran (RB), sorghum, soybean meal (SBM), sunflower meal (SFM), and wheat. Methods: Two cohorts of 36 pigs each (initial body weight = $78.5{\pm}3.7kg$) were randomly assigned to 2 rooms, each housing 36 pigs, and then allotted to 6 diets with 6 replicates per diet in a randomized complete block design. Test ingredient was the only dietary source of P and diets contained 6 concentrations of phytase (0, 125, 250, 500, 1,000, or 2,000 phytase units [FTU]/kg) with 0.4% of $TiO_2$ as a digestibility marker. Feeding schedule for each ingredient was 5 d acclimation, 5 d fecal collection, and 4 d washout. The STTD of P increased (linear or exponential $p{\leq}0.001$) with the inclusion of phytase for all ingredients. Results: Basal STTD of P was 37.6% for CM, 37.6% for corn, 68.6% for DDGS, 10.3% for RB, 41.2% for sorghum, 36.7% for SBM, 26.2% for SFM, and 55.1% for wheat. The efficiency of this novel phytase to hydrolyze phytate is best described with a broken-line model for corn, an exponential model for CM, RB, SBM, SFM, and wheat, and a linear model for DDGS and sorghum. Based on best-fit model the phytase dose (FTU/kg) needed for highest STTD of P (%), respectively, was 735 for 64.3% in CM, 550 for 69.4% in corn, 160 for 55.5% in SBM, 1,219 for 57.8% in SFM, and 881 for 64.0% in wheat, whereas a maximum response was not obtained for sorghum, DDGS and RB within the evaluated phytase range of 0 to 2,000 FTU/kg. These differences in the phytase concentration needed to maximize the STTD of P clearly indicate that the enzyme does not have the same hydrolysis efficiency among the evaluated ingredients. Conclusion: Variations in enzyme efficacy to release P from phytate in various feedstuffs need to be taken into consideration when determining the matrix value for phytase in a mixed diet, which likely depends on the type and inclusion concentration of ingredients used in mixed diets for pigs. The use of a fixed P matrix value across different diet types for a given phytase concentration is discouraged as it may result in inaccurate diet formulation.

• Journal of Life Science
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• 제18권1호
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• pp.52-57
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• 2008

Xylan is a major hemicellulose component of the cell walls of monocots and hardwood, representing up to 30% of the dry weight of these plants. To efficiently hydrolyze xylan, the endoxylanase gene from Bacillus sp. was expressed in B. subtilis DB431 by introducing the plasmid pJHKJ4. The total activity of the recombinant endoxylanase reached about 857 unit/ml by batch fermentation of B. subtilis DB431/pJHKJ4 in LB maltose medium. The majority (>92%) of endoxylanase was efficiently secreted into the culture medium. The recombinant endoxylanase hydrolyzed more the birchwood xylan efficiently than the other xylans. When 4 % concentration of xylan was used, the highest production of xylooligosaccharide was observed, and xylobiose and xylotriose were the major products. Optimal amount of enzyme and reaction time for producing xylooligosaccharide were found to be 10 unit and 1 hr, respectively. In addition, the temperature of $40^{\circ}C{\sim}50^{\circ}C$ gave the highest production of xylooligosaccharide. Consequently, the optimized conditions for the production of xylooligosaccharide through the hydrolysis of xylan were determined as follows: 10 unit endoxylanase, $50^{\circ}C$, 4% birchwood xylan, 1 hr reaction.

• Journal of Microbiology and Biotechnology
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• 제24권7호
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• pp.943-953
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• 2014

The XylH gene (1,167-bp) encoding a novel hemicellulase (41,584 Da) was identified from the genome of Microbacterium trichothecenolyticum HY-17, a gastrointestinal bacterium of Gryllotalpa orientalis. The enzyme consisted of a single catalytic domain, which is 74% identical to that of an endo-${\beta}$-1,4-xylanase (GH10) from Isoptericola variabilis 225. Unlike other endo-${\beta}$-1,4-xylanases from invertebrate-symbiotic bacteria, rXylH was an alkali-tolerant multifunctional enzyme possessing endo-${\beta}$-1,4-xylanase activity together with ${\beta}$-1,3/${\beta}$-1,4-glucanase activity, which exhibited its highest xylanolytic activity at pH 9.0 and 60oC, and was relatively stable within a broad pH range of 5.0-10.0. The susceptibilities of different xylosebased polysaccharides to the XylH were assessed to be as follows: oat spelts xylan > beechwood xylan > birchwood xylan > wheat arabinoxylan. rXylH was also able to readily cleave p-nitrophenyl (pNP) cellobioside and pNP-xylopyranoside, but did not hydrolyze other pNP-sugar derivatives, xylobiose, or hexose-based materials. Enzymatic hydrolysis of birchwood xylan resulted in the product composition of xylobiose (71.2%) and xylotriose (28.8%) as end products.

• Bulletin of the Korean Chemical Society
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• 제30권5호
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• pp.1152-1156
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• 2009

Silent information regulator 2 (Sir2) or sirtuins are NAD(+)-dependent deacetylases, which hydrolyze the acetyllysine residues. In mammals, sirtuins are classified into seven different classes (SIRT1-7). SIRT1 was reported to be involved in age related disorders like obesity, metabolic syndrome, type II diabetes mellitus and Parkinson’s disease. Activation of SIRT1 is one of the promising approaches to treat these age related diseases. In this study, we have used HipHop module of CATALYST to identify a series of pharmacophore models to screen SIRT1 enhancing molecules. Three molecules from Sirtris Pharmaceuticals were selected as training set and 607 sirtuin activator molecules were used as test set. Five different hypotheses were developed and then validated using the training set and the test set. The results showed that the best pharmacophore model has four features, ring aromatic, positive ionization and two hydrogen-bond acceptors. The best hypothesis from our study, Hypo2, screened high number of active molecules from the test set. Thus, we suggest that this four feature pharmacophore model could be helpful to screen novel SIRT1 activator molecules. Hypo2-virtual screening against Maybridge database reveals seven molecules, which contains all the critical features. Moreover, two new scaffolds were identified from this study. These scaffolds may be a potent lead for the SIRT1 activation.

• Journal of Life Science
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• 제27권9호
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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 Clinical Laboratory Science
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• 제38권3호
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• pp.166-172
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• 2006

Metallo-${\beta}$-lactamase (MBL) can hydrolyze all ${\beta}$-lactams except monobactams and frequently coexists with various antibiotic resistance genes such as aminoglycoside resistance, sulfonamide resistance gene, etc. Therefore, the effective antibiotics against infections by these bacteria are markedly limited or can't even be found. We tried to search in-vitro antimicrobial combinations with synergistic effects for a VIM-2 type MBL producing Pseudomonas aeruginosa, isolated from clinical specimen. On the selection of antibiotic combinations with synergistic effects, we performed a one disk synergy test, modified Pestel's method, in agar without aztreonam (AZT). The bacteriostatic synergistic effects of this tests were scored as $S_1$ (by susceptibility pattern in agar without antibiotics), $S_2$ (by the change of susceptibility in agar with or without antibiotics) and $S_3$ ($S_1$ + $S_2$) and was classified into weak (1 point), moderate (2 points) and strong (3 points) by $S_3$ score. Subsequently, we carried out the time-killing curve for the antibiotic combinations with the strong synergistic bacteriostatic effect. One VIM-2 type MBL producing P. aeruginosa confirmed by the PCR showed all resistance against all ${\beta}$-lactams except AZT, aminoglycoside and ciprofloxacin. In the one disk synergy test, this isolate showed a strong bacteriostatic synergistic effect for the antibiotic combination of AZT and piperacillin-tazobactam (PIP-TZP) or AZT and amikacin (AN). On the time-killing curve after six hours of incubation, the colony forming units (CFUs/mL) of this bacteria in the medium broth with both combination antibiotics were decreased to 1/18.7, 1/17.1 of the least CFUs of each single antibiotics. The triple antibiotic combination therapy including AZT, PIP-TZP and AN was shown to be significantly synergistic after 8 hrs of exposure. In a VIM-2 MBL producing P. aeruginosa with susceptibility for AZT, the triple antibiotic combination therapy including AZT, PIP-TZP and AN may be considered as an alternative antibiotics modality against the infection by some MBL type. But the antimicrobial combination therapy for many more MBL producing isolates is essential to know as soon as possible for the selection of effective treatment against the infection by this bacteria.

• Microbiology and Biotechnology Letters
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• 제48권2호
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• pp.158-166
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• 2020

A gene coding for the xylanase was cloned from Paenibacillus woosongensis, followed by determination of its complete nucleotide sequence. This xylanase gene, designated as xyn10A, consists of 1,446 nucleotides encoding a polypeptide of 481 amino acid residues. Based on the deduced amino acid sequence, Xyn10A was identified to be a modular enzyme composed of a catalytic domain highly homologous to the glycosyl hydrolase family 10 xylanase and a putative carbohydrate-binding module (CBM) in the C-terminus. By using DEAE-sepharose and phenyl-sepharose column chromatography, Xyn10A was purified from the cellfree extract of recombinant Escherichia coli carrying a P. woosongensis xyn10A gene. The N-terminal amino acid sequence of the purified Xyn10A was identified to exactly match the sequence immediately following the signal peptide predicted by the Signal5.0 server. The purified Xyn10A was a truncated protein of 33 kDa, suggesting the deletion of CBM in the C-terminus by intracellular hydrolysis. The purified enzyme had an optimum pH and temperature of 6.0 and 55-60℃, respectively, with the kinetic parameters V_max and K_m of 298.8 U/mg and 2.47 mg/ml, respectively, for oat spelt xylan. The enzyme was more active on arabinoxylan than on oat spelt xylan and birchood xylan with low activity for p-nitrophenyl-β-xylopyranoside. Xylanase activity was significantly inhibited by 5 mM Cu²⁺, Mn²⁺, and SDS, and was noticeably enhanced by K⁺, Ni²⁺, and Ca²⁺. The enzyme could hydrolyze xylooligosaccharides larger than xylobiose. The predominant products resulting from xylooligosaccharide hydrolysis were xylobiose and xylose.

• Microbiology and Biotechnology Letters
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• 제48권2호
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• pp.215-222
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• 2020

The marine microorganism PX-1, which can hydrolyze xylan, was isolated from coastal sea water of Jeju Island, Korea. Based on the 16S rRNA gene sequence and chemotaxonomy analysis, PX-1 was identified as a species of the genus Aestuariibacter and named Aestuariibacter sp PX-1. From the culture broth of PX-1, an extracellular xylanase was purified to homogeneity through ammonium sulfate precipitation and subsequent adsorption chromatography using insoluble xylan. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration chromatography estimated the molecular weight of the purified putative xylanase (XylA) as approximately 64 kDa. XylA showed xylanase activity toward beechwood xylan, with a maximum enzymatic activity at pH 6.0 and 45℃. Through thin-layer chromatographic analysis of the xylan hydrolysate produced by XylA, it was confirmed that XylA is an endo-type xylanase that decomposes xylan into xylose and xyloligosaccharides of various lengths. The K_m and V_max values of XylA for beechwood xylan were 27.78 mM and 78.13 μM/min, respectively.