• 동아시아식생활학회지
• /
• 제25권3호
• /
• pp.513-524
• /
• 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.

• Animal Bioscience
• /
• 제35권11호
• /
• pp.1744-1751
• /
• 2022

Objective: The present study aimed to investigate the effect of xylo-oligosaccharides (XOS) administration on egg production, reproductive hormones, serum lipids and adipokines of hens at the late cycle of reproduction. Methods: Four treatments included control (basal diet) and XOS addition at 2.0 (XOS-2), 4.0 (XOS-4), or 6.0 (XOS-6) g/kg of diet using 288 commercial Hy-Line brown hens from 73 to 84 wk of age. Egg production, body fat deposition, reproductive tract and hormones, lipid metabolism and adipokines were determined. Results: At 84 wk, compared to the control, XOS supplementation at the three doses increased (p<0.001) egg-laying rates by 13.2% averagely, which led to a higher egg mass by 131 g/hen throughout the whole trial period. Abdominal fat and skinfold of XOS treatments were decreased (p<0.001) by 26.1% and 18.6%, respectively; large follicles and ovary weight were increased (p<0.001) by 0.73 follicle/hen and 18.6%, respectively. For serum parameters, cholesterol and triglyceride were decreased (p<0.001) by 17.5% and 29.2%, respectively; luteinizing hormone, follicle-stimulating hormone, and progesterone were increased (p≤0.001) by 16%, 31%, 29%, respectively; adiponectin and visfatin were increased (p<0.001) by 34% and 44%, respectively; but chemerin and leptin were decreased (p≤0.001) by 22% and 14%, respectively. With the increased XOS doses, linear decreases (p<0.05) were found on abdominal skinfold and serum triglyceride. Conclusion: The obtained data indicate that XOS can be used as an additive to improve fecundity by beneficially modulating fat deposition, lipid metabolism, reproductive hormones, and adipokines of hens at the late cycle of reproduction.

• Journal of Microbiology and Biotechnology
• /
• 제25권9호
• /
• pp.1476-1484
• /
• 2015

Three endoxylanase-encoding genes from the moderately themophilic chemoorganotrophic bacterium Melioribacter roseus were cloned and expressed in Escherichia coli. Genes xyl2091 (Mros_2091) and xyl2495 (Mros_2495) encode GH10 family hydrolases, whereas xyl2090 (Mros_2090) represents the GH30 family. In addition to catalytic domains, Xyl2090 and Xyl2091 contain carbohydrate-binding modules that could facilitate their binding to xylans and Por sorting domains associated with the sorting of proteins from the periplasm to the outer membrane, where they are covalently attached. Recombinant endoxylanase Xyl2495 exhibited a high specific activity of 1,920 U/mg on birchwood xylan at 40℃. It is active at low temperatures, exhibiting more than 30% of the maximal activity even at 0℃. Endoxylanases Xyl2090 and Xyl2091 have lower specific activities but higher temperature optima at 80℃ and 65℃, respectively. Analysis of xylan hydrolysis products revealed that Xyl2090 generates xylo-oligosaccharides longer than xylopentaose. Xylose and xylobiose are the major products of xylan hydrolysis by the recombinant Xyl2091 and Xyl2495. No activity against cellulose was observed for all enzymes. The presence of three xylanases ensures efficient xylan hydrolysis by M. roseus. The highly processive "free" endoxylanase Xyl2495 could hydrolyze xylan under moderate temperatures. Xylan hydrolysis at elevated temperatures could be accomplished by concerted action of two cell-bound xylanases; Xyl2090 that probably degrades xylans to long xylo-oligosaccharides, and Xyl2091 hydrolyzing them to xylose and xylobiose. The new endoxylanases could be useful for saccharification of lignocellulosic biomass in biofuels production, bleaching of paper pulp, and obtaining low molecular weight xylooligosaccharides.

• Journal of the Korean Wood Science and Technology
• /
• 제40권2호
• /
• pp.123-132
• /
• 2012

Pre-pulping extracts were found to contain a dilute amount of xylo-oligosaccharides and acetic acid as the major components, and many minor components including other organic acids, lignin-derived phenolics, and sugar degradation products. Once separated from the pulp, a secondary hydrolysis step was required to hydrolyze oligomeric hemicellulose sugars into monomeric sugars before fermentation. The following study detailed the extent of hemicellulose recovery by pre-pulping using hot water extraction and characterized the hydrolysis of the extract with respect to comparing acid and enzymatic hydrolysis. The secondaryhydrolysis of hot water extracts made at an H-Factor of 800 was tested for a variety of acid and enzyme loading levels using the sulfuric acid and xylanases. The maximum fermentable sugar yield from acid and enzyme hydrolysis of the extract was 18.7 g/${\ell}$ and 17.7 g/${\ell}$ representing 84.6% and 80.1% of the maximum possible yield, respectively.

• 한국식품과학회지
• /
• 제48권3호
• /
• pp.201-207
• /
• 2016

메밀껍질은 메밀 알곡보다 유효성분이 많음에도 불구하고 식품학적 가치가 떨어져 대부분 폐기되고 있다. 따라서 이를 기능성 식품소재로 활용하기 위해 효소분해하여 기능성 올리고당을 생산하고 이들의 특성을 분석하였다. 올리고당 생산을 위한 최적 가수분해조건은 셀룰로스 분획의 경우 pH 5.0, $40^{\circ}C$, 기질농도 4%로 결정되었으며, 헤미셀룰로스 분획은 pH 5.0, $40^{\circ}C$, 30 unit으로 결정되었다. 최적 분해조건을 이용하여 72시간 효소분해 후 얻은 올리고당의 생산량을 측정한 결과, 셀룰로스와 헤미셀룰로스 분획으로부터 얻은 올리고당의 수율은 각각 132.37 g/kg 및 393.04 g/kg이었다. 또한 각 분획의 올리고당 함량을 측정한 결과, 포도당, 자일로스, xylobiose, xylotriose, cellobiose 및 cellotriose가 검출되었다. 올리고당(OSC, OSH)의 산화방지 활성을 측정한 결과, OSC는 분해시간이 증가할수록 산화방지 활성은 감소한 반면 OSH는 증가하였다. 또한 메밀껍질로부터 생산된 올리고당 첨가 시, 모든 비피더스 균주의 생육이 control에 비해 증가하여 프리 바이오틱 효과가 있음을 알 수 있었다. 이상의 연구결과, 효소분해에 의해 메밀껍질로부터 올리고당을 생산할 수 있었으며, 산화방지와 프리바이오틱 효과가 있음을 확인하였다. 따라서 목적에 따라 효소의 처리시간 및 방법을 다양화한다면 기능성식품으로의 활용이 더 높아질 것으로 예상된다.

• Journal of Microbiology and Biotechnology
• /
• 제32권2호
• /
• pp.187-194
• /
• 2022

Two α-ʟ-arabinofuranosidases (BfdABF1 and BfdABF3) and a β-ᴅ-xylosidase (BfdXYL2) genes were cloned from Bifidobacterium dentium ATCC 27679, and functionally expressed in E. coli BL21(DE3). BfdABF1 showed the highest activity in 50 mM sodium acetate buffer at pH 5.0 and 25℃. This exo-enzyme could hydrolyze p-nitrophenyl arabinofuranoside, arabino-oligosaccharides (AOS), arabinoxylo-oligosaccharides (AXOS) such as 3²-α-ʟ-arabinofuranosyl-xylobiose (A³X), and 2³-α-ʟ-arabinofuranosyl-xylotriose (A²XX), whereas hardly hydrolyzed polymeric substrates such as debranched arabinan and arabinoxylans. BfdABF1 is a typical exo-ABF with the higher specific activity on the oligomeric substrates than the polymers. It prefers to α-(1,2)-ʟ-arabinofuranosidic linkages compared to α-(1,3)-linkages. Especially, BfdABF1 could slowly hydrolyze 2³,3³-di-α-ʟ-arabinofuranosyl-xylotriose (A²⁺³XX). Meanwhile, BfdABF3 showed the highest activity in sodium acetate at pH 6.0 and 50℃, and it has the exclusively high activities on AXOS such as A³X and A²XX. BfdABF3 mainly catalyzes the removal of ʟ-arabinose side chains from various AXOS. BfdXYL2 exhibited the highest activity in sodium citrate at pH 5.0 and 55℃, and it specifically hydrolyzed p-nitrophenyl xylopyranoside and xylo-oligosaccharides (XOS). Also, BfdXYL2 could slowly hydrolyze AOS and AXOS such as A³X. Based on the detailed hydrolytic modes of action of three exo-hydrolases (BfdABF1, BfdABF3, and BfdXYL2) from Bf. dentium, their probable roles in the hemiceullose-utilization system of Bf. dentium are proposed in the present study. These intracellular exo-hydrolases can synergistically produce ʟ-arabinose and ᴅ-xylose from various AOS, XOS, and AXOS.

• Journal of Microbiology and Biotechnology
• /
• 제8권1호
• /
• pp.28-33
• /
• 1998

A gene coding for ${\beta}$-xylosidase from thermophilic xylanolytic Bacillus sp. KK-1 was cloned into Escherichia coli using plasmid pBR322. Recombinant plasmid DNAs were isloated from E. coli clones which were capable of hydrolyzing 4-methylumbelliferyl-${\beta}$-D xylopyranoside. Restriction analysis showed the DNAs to share a common insert DNA. Xylo-oligosaccharides, including xylotriose, xylotetraose, xylopentaose, and xylobiose were hydrolyzed to form xylose as an end product by cell-free extracts of the E. coli clones, confirming that the cloned gene from strain KK-1 is ${\beta}$-xylosidase gene. The ${\beta}$-xylosidase gene of strain KK-1 designated as xylB was completely sequenced. The xylB gene consisted of an open reading frame of 1,602 nucleotides encoding a polypeptide of 533 amino acid residues, and a TGA stop codon. The 3' flanking region contained one stem-loop structure which may be involved in transcriptional termination. The deduced amino acid sequence of the KK-1 ${\beta}$-xylosidase was highly homologous to the ${\beta}$-xylosidases of Bacillus subtilis and Bacillus pumilus, but it showed no similarity to a thermostable ${\beta}$-xylosidase from Bacillus stearothermophilus.

• 한국미생물·생명공학회지
• /
• 제24권2호
• /
• pp.197-205
• /
• 1996

The $\beta$-xylosidase was purified 99- fold from the culture supernatant of Pseudo onas sp. CB-33 by ammonium sulfate precipitation, PEI precipita- tion, DEAE-Sephadex column chromatography, Sephadex G-75 gel filtration chromatography and preparative disc gel electrophoresis. Molecular weight of the enzyme was estimated to be 44,000 by SDS polyacrylamide gel electrophoresis. The enzyme has a pH optimum for activity at 7.0 and is stable over pH 6.5-9.0. The optimal temperature of the enzyme was 45$\circ$C, and its enzymatic activity was completely inactivated at 55$\circ$C for 30 min. Km value of the enzyme for p-nitrophenyl-$\beta$-D-xylopyranoside was calculated to be 4.6 mM. The effect of various reagents on the $\beta$-xylosidase activity was investigated. The enzyme activity was completely inhibited by Hg$^{2+}$, Cu$^{2+}$ and Zn$^{2+}$. The $\beta$-xylosidase was inactivated by tryptophan-specific reagent, N-bromosuccinimide and tyrosine-specific reagent, iodine. The enzyme could degrade xylo-oligosaccharides to xylose and the enzyme was competitively inhibited by xylose. The $\beta$-xylosidase and endoxylanase from Psedomonas sp. CB-33 hydrolized xylan synergically. The purified enzyme also showed $\alpha$-L-arabinofuranosidase activity.

• 한국미생물·생명공학회지
• /
• 제20권5호
• /
• pp.574-582
• /
• 1992

Bacillus stearothermophilus exo-xylanase 유전자 DNA가 삽입된 재조합 plasmid pMG1을 가지고 있는 E.coli JM109 exo-xylanase 생산 최적 배양 조건, 생산 효소의 정제 및 정제 효소의 특성 등을 조사 연구하였다. 상기 재조합 E.coli 균주는 0.5 fructose, 0.5 yeast extract, 1.0 tryptone 및 1.0 sodium chloride가 함유된 배지에서 약 10시간 배양했을 때 최대량의 효소를 생산하였으며 생산효소의 94는 세포내에 존재하는 것으로 분석되었다. 생산 효소는 ammonium sulfate 분획, ion exchange chromatography 및 gel filtration 등의 과정을 거쳐 단일 단백질로 정제하였으며 정제 효소는 pH 6.0과 $45^{\circ}C$에서 가장 높은 효소 활성을 나타내었다.또한 1mM $Ca^{2+}$과 $Co^{2+}$ 이온의 첨가는 각각 약 25% 정도의 활성화 효과를 나타내는 반면, 본 효소의 pNPX에 대한 $K_{m}$은 2.75mM, pl값을 4.7, 그리고 분자량은 gel-filtration 법으로는 약 200,000dal., SDS-polyacrylamide gel 전기영동법으로는 약 66,000dal 으로 측정되어 세 개의 동일한 subunit로 구성된 효소 단백질인 것으로 추정되었다. 본 정제 효소는 xylobiose, xylotrioxe 및 xylotetraose 등의 xylo-oligosaccharide를 효과적으로 분해함은 물론이고, 분해율은 낮으나 birchwood xylan, larchwood xylan 및 oatspelt xylan 등의 xyland에도 작용, xylose 생산을 확인함으로써 본 효소는 그 예가 극히 드문 bacterial exo-xylanase인 것으로 분류되었다.