• Title/Summary/Keyword: Fermentable Protein

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Loss of ARID1A Expression in Gastric Cancer: Correlation with Mismatch Repair Deficiency and Clinicopathologic Features

  • Kim, Kyung-Ju;Jung, Hae Yoen;Oh, Mee-Hye;Cho, Hyundeuk;Lee, Ji-Hye;Lee, Hyun Ju;Jang, Si-Hyong;Lee, Moon Soo
    • Journal of Gastric Cancer
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    • v.15 no.3
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    • pp.201-208
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    • 2015
  • Purpose: The AT-rich interactive domain 1A (ARID1A ) gene encodes BRG1-associated factor 250a, a component of the SWItch/Sucrose NonFermentable chromatin remodeling complex, which is considered a tumor suppressor in many tumors. We aimed to investigate the prognostic significance of ARID1A expression in gastric cancers and explore its relationship with clinicopathologic parameters such as mismatch repair protein expression. Materials and Methods: Four tissue microarrays were constructed from 191 resected specimens obtained at Soonchunhyang University Cheonan Hospital from 2006 to 2008. Nuclear expression of ARID1A was semiquantitatively assessed and binarized into retained and lost expression. Results: Loss of ARID1A expression was observed in 62 cases (32.5%). This was associated with more frequent vascular invasion (P=0.019) and location in the upper third of the stomach (P=0.001), and trended toward more poorly differentiated subtypes (P=0.054). ARID1A loss was significantly associated with the mismatch repair-deficient phenotype (P=0.003). ARID1A loss showed a statistically significant correlation with loss of MLH1 (P=0.001) but not MSH2 expression (P=1.000). Kaplan-Meier survival analysis showed no statistically significant difference in overall survival; however, patients with retained ARID1A expression tended to have better overall survival than those with loss of ARID1A expression (P=0.053). In both mismatch repair-deficient and mismatch repair-proficient groups, survival analysis showed no differences related to ARID1A expression status. Conclusions: Our results demonstrated that loss of ARID1A expression is closely associated with the mismatch repair-deficient phenotype, especially in sporadic microsatellite instability-high gastric cancers.

Studies on Sikhye Wine -2. Glutinous Rice Sikhye Wine- (식혜주에 관한 연구 -2보. 찹쌀식혜 올리고당주-)

  • 안용근;김승겸;신철승
    • The Korean Journal of Food And Nutrition
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    • v.10 no.3
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    • pp.365-369
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    • 1997
  • Glutinous rice Sikhye was fermented by Saccharomyces cerevisiae for 10 day at 29$^{\circ}C$. Fermentable sugars such as maltose and maltotriose in glutinous rice Sikhye were converted into ethanol by the yeast, but limit dextrin was remained after the fermentation. fermentation rate of sugars in glutinous rice Sikhye was lower than that in rice Sikhye. Glutinous rice Sikhye wine was found to contain 7.3% of limit dextrin, 3.6% of ethanol, 0.35$\mu$mol/ml of amino acid, 100$\mu\textrm{g}$/ml of protein, and the acidity of the Sikhye showed 3.2, respectively, and its pH was 3.23. Limit dextrin in glutinous rice Sikhye wine showed both signal of $\alpha$-1, 4- and $\alpha$-1,6- glucisidic linkage with its estimation ratio of 5.6:1 by 1H-NMR analysis. The taste of rice Sikhye wine was similar that of wine.

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The Production of Xanthan from Brewer's Spent Grain

  • Rajiv Chetia;Bhriganka Bharadwaj;Rahul Dey;Biswa Prasun Chatterji
    • Microbiology and Biotechnology Letters
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    • v.51 no.4
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    • pp.449-456
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    • 2023
  • Sugar or dextrose increases the cost of production of xanthan gum by Xanthomonas campestris. Brewers' Spent Grain (BSG) was chosen as a source of fermentable sugars. BSG is a significant industrial by-product generated in large quantities from the breweries. Primarily used as animal feed due to its high fiber and protein content, BSG holds great potential as an economically and ecologically sustainable substrate for fermenting biomolecules. This study explores BSG's potential as a cost-effective carbon source for producing xanthan, utilizing Xanthomonas campestris NCIM 2961. An aqueous extract was prepared from BSG and inoculated with the bacterium under standard fermentation conditions. After fermentation, xanthan gum was purified using a standard protocol. The xanthan yield from BSG media was compared to that from MGYP media (control). The fermentation parameters, including pH, temperature, agitation and duration were optimized for maximum xanthan gum yield by varying them at different levels. Following fermentation, the xanthan gum was purified from the broth by alcoholic precipitation and then dried. The weight of the dried gum was measured. The obtained xanthan from BSG under standard conditions and commercial food-grade xanthan were characterized using FTIR. The highest xanthan yields were achieved at 32 ℃, pH 6.0, and 72 h of fermentation at 200 rpm using BSG media. The FTIR spectra of xanthan from BSG media closely resembled that of commercial food-grade xanthan. The results confirm the potential of BSG as a cost-effective alternative carbon source for xanthan production, thereby reducing production costs and solid waste.

Effects of Passtein® Supplements on Protein Degradability, Ruminal Fermentation and Nutrient Digestibility (패스틴®첨가가 단백질 분해율과 반추위 발효 및 영양소 소화율에 미치는 영향)

  • Choi, Y.J.;Choi, N.J.;Park, S.H.;Song, J.Y.;Um, J.S.;Ko, J.Y.;Ha, J.K.
    • Journal of Animal Science and Technology
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    • v.44 no.5
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    • pp.549-560
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    • 2002
  • This study, including two in vitro experiments and an in vivo experiment were conducted to evaluate effects of Passtein$^{(R)}$ on crude protein degradability, ruminal fermentation characteristics and nutrient digestibility. In in vitro experiment protein degradability was examined using borate-phosphate buffer and neutral detergent, and using protease from Stroptomyces griseus at 39$^{\circ}C$ for 0, 2, 4, 8, 12, and 48 h. In addition, an in vivo experiment was conducted in a switch back design and ruminal fermentation and nutrient digestibility were determined. Four ruminal-fistulated Holstein cows weighing 300kg in mean body weight randomly allotted to 2 treatments (control and Passtein$^{(R)}$ supplementation). Although there was no significant difference on protein fraction between treatments, it appears that Passtein$^{(R)}$ supplementation decreased buffer soluble protein fraction compared to control. Protein degradability was not affected by Passtein$^{(R)}$ from 0 h to 4 h, but decreased at 12 h and 48 h compared to control. Degradation of immediately degradable fraction was higher in Passtein$^{(R)}$ treatment, but degradation of fermentable fraction was lower in Passtein$^{(R)}$ treatment compared to control. The pH and $NH_3$-N concentration tended to increase in Passtein$^{(R)}$ treatment, but VFA production, microbial counts and enzyme activity tended to decrease in Passtein$^{(R)}$ treatment compared to control. In addition, nutrient digestibility in the total tract tended to increase in Passtein$^{(R)}$ treatment compared to control.

Fermentable and Nutritional Characteristics of Brewery Meal-Based Fermented Feedstuffs Supplemented with Aspergillus Oryzae and Saccharomyces Cerevisiae (Aspergillus Oryzae 및 Saccharomyces Cerevisiae를 첨가하여 제조한 맥주박 위주 발효사료의 발효 특성 및 영양학적 특성)

  • Shin, Jong-Suh;Park, Byung-Ki;Kim, Byong-Wan
    • Journal of The Korean Society of Grassland and Forage Science
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    • v.25 no.4
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    • pp.297-306
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    • 2005
  • This study was conducted to compare and evaluate fermentable and nutritional characteristics of brewery meal-based fermented feedstuffs supplemented with Aspergillus oryzae (AO) and Saccharomyces cerevisiae (SC). Experiments were divided into three treatment groups; fermented feedstuff supplemented with $1\%$ of AO(FFAO), fermented feedstuff supplemented with $1\%$ of SC(FFSC), and fermented feedstuff supplemented with $0.5\%$ of AO and $0.5\%$ of SC(FFAS). For changes of crude protein contents by 48 h fermentation, there were no significant differences among treatments. Ether extract(EE) contents were significantly increased by 48 h fermentation (p<0.05). Neutral detergent fiber(NDF) contents of FFAO, FFSC and FFAS were significantly decreased by 48 h fermentation(p<0.05), but acid detergent fiber(ADF) and acid detergent lignin (ADL) contents were not different. The pH of FFAO and FFAS was decreased more rapidly than that of FFSC(p<0.05), reaching a plateau after 24 h. Alcohol content was increased rapidly until 18 h in FFAO and was increased rapidly until 12 h in FFSC and FFAS, and alcohol content of FFAO, FFSC and FFAS was maintained constantly after 24 h. The ammonia N content of FFAO, FFSC and FFAS was 0.022, 0.073 and $0.040\%$ at 48 h, respectively, and then ammonia N was over twice higher in FFSC than in FFAO and FFAS(p<0.05). Dextrose content was increased until 6 h in FFAO but was rapidly decreased in FFSC and FFAS until 6 h(p<0.05). Lactate content was higher in FFAO and FFAS than in FFSC(p<0.05). Consequently, when we added AO in formulation of fermented feedstuff with brewery meal which moisture content was high, EE, alcohol, and lactate contents were increased, but NDF and ammonia N contents were reduced. Therefore, it is expected that AO will be effective to increase the feed value and the preservation of fermented feedstuff with a high moisture content.

Electrostatic Immobilization of D-Xylose Isomerase to a Cation Exchanger for the Conversion of D-Xylose to D-Xylulose (D-xylose에서 D-xylulose로의 전환을 위한 D-xylose Isomerase의 정전기적 고정화)

  • Hang, Nguyen Thi;Kim, Sung-Gun;Kweon, Dae-Hyuk
    • Microbiology and Biotechnology Letters
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    • v.40 no.2
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    • pp.163-167
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    • 2012
  • Since D-xylose is not fermentable in Saccharomyces cerevisiae, its conversion to D-xylulose is required for its application in biotechnological industries using S. cerevisiae. In order to convert D-xylose to D-xylulose by way of an enzyme immobilized system, D-xylose isomerase (XI) of Escherichia coli was fused with 10-arginine tag (R10) at its C-terminus for the simple purification and immobilization process using a cation exchanger. The fusion protein XIR10 was overexpressed in recombinant E. coli and purified to a high purity by a single step of cation exchange chromatography. The purified XIR10 was immobilized to a cation exchanger via the electrostatic interaction with the C-terminal 10-arginine tag. Both the free and immobilized XIR10 exhibited similar XI activities at various pH values and temperatures, indicating that the immobilization to the cation exchanger has a small effect on the enzymatic function of XIR10. Under optimized conditions for the immobilized XIR10, D-xylose was isomerized to D-xylulose with a conversion yield of 25%. Therefore, the results of this study clearly demonstrate that the electrostatic immobilization of XIR10 via the interaction between the 10-arginine tag and a cation exchanger is an applicable form of the conversion of D-xylose to D-xylulose.