• Title/Summary/Keyword: 2.5% sucrose

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Effect of Preservative Solutions on Flowering and Vase Life of Multiflowered Cut Lily (Lilium longiflorum Thunb.) (일경다화성(一莖多花性) 백합(百合) 절화(切花)의 개화(開花)와 수명연장(壽命延長)을 위(爲)한 보존용액(保存溶液)의 효과(效果))

  • Lee, Jong Suk;Kim, Young Rae;Ku, Ja Hyeong
    • Korean Journal of Agricultural Science
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    • v.10 no.2
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    • pp.249-256
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    • 1983
  • The aspect of flowering was investigated in 'Georgia' cut lilies which had four flowers per stem. Concurrently effects of preservative solutions on longevity, petal length, water uptake and fresh weight of cut flowers were examined. 1. Days of opening of the 1st, 2nd and 3rd flower were 1-2 days, 3-4 days and 5-6days after beginning of holding treatment respectively. But the 4th flower was opened 9-10 days after beginning of holding treatment when the 1st and 2nd flowers were wilting or drying. 2. The later the opening of flower in a stem was, the shorter the longevity of flower became. But the effects of preservative solutions on longevity were gradually increased as the opening of flower was late in a stem. 3. Preservative solutions containing sucrose and $AgNO_3$ or HQ were able to increase petal length and longevity of the 3rd and 4th flowers sufficiently like the 1st and 2nd flowers. 4. Petal length, water uptake, fresh weight and longevity of cut lilies held in preservative solution containing sucrose, $AgNO_3$ and HQ were increased significantly compared with others. Solution containing sucrose alone increased longevity but decreased water uptake remarkably and did not increase fresh weight and petal length effectively compared with the control.

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Cryopreservation of in vitro-cultured Axillary Shoot Tips of Japanese Bead Tree (Melia azedarach) using Vitrification Technique

  • Yang Byeong-Hoon;Kim Hyun-Tae;Park Ju-Yong;Park Young-Goo
    • Korean Journal of Plant Resources
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    • v.19 no.3
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    • pp.385-391
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    • 2006
  • In vitro-grown axillary buds of Melia aredarach were successfully cryopreserved by vitrification. On the MS medium supplemented with BA 1 mg/L, multiple shoots were developed within $4{\sim}5$ weeks. Plantlets of Melia azedarach were cold-hardened at $10^{\circ}C$ for a 16-hr photo-period for 6 weeks. Excised axillary shoot-tips from hardened plantlets were precultured on a solidified Murashige & Skoog agar medium (MS) supplemented with 0.7 M sucrose for 1 day at $25^{\circ}C$. Axillary shoot-tip meristems wert dehydrated using a highly concentrated vitrification solution (PVS2) for 60 min at $0^{\circ}C$ prior to a direct plunge into liquid nitrogen (LN). The PVS2 vitrification solution consisted of 30% glycerol (w/v), 15% ethylene glycol (w/v), 15% DMSO (w/v) in MS medium containing 0.4M sucrose. After short-term warming in a water bath at $40^{\circ}C$, the meristems were transferred into 2 ml of MS medium containing 1.2M sucrose for 15 min and then planted on solidified MS culture medium. Successfully vitrified and warmed meristems resumed growth within 2 weeks and directly developed shoots without intermediary callus formation. The survival rate of cold-hardened plantlets for 3 and 4 weeks was 90%. We did not find any difference in PCR-band patterns between control and cryopreserved plants. This method appears to be a promising technique for cryopreserving axillary shoot-tips from in vitro-grown plantlets of Medicinal plants.

Candidate Genes Related to Sugar Content in Sweetpotato using GWAS

  • Tae Hwa Kim;Mi Nam Chung;Hyeong Un Lee;Won Park;Sang Sik Nam
    • Proceedings of the Korean Society of Crop Science Conference
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    • 2022.10a
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    • pp.192-192
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    • 2022
  • Sweetpotato is rich in starch, which is converted to sugar during storage due to enzymatic hydrolysis. The sugar content of sweetpotato is a component related to taste and storability. In this study, the sugar content (fructose, glucose, maltose, sucrose and total sugar content) of 94 genotypes was evaluated and the GWAS (Genome-Wide Association Study) was conducted to search for candidate genes for sugar content. The fructose and glucose content were 0.2 ~ 8.8 and 0.2 ~ 9.4 g/100g, respectively. The maltose, sucrose and total sugar content were 0.2 ~ 9.1,3.2 - 30.0 and 7.9 ~ 40.2 g/100g, respectively. The fructose and glucose showed a positive correlation (0.98). The 94 genotypes were genotyped with genotyping-by-sequencing (GBS) and aligned against the reference genome sequences of sweetpotato. The GBS libraries from 94 genotypes were sequenced on an Illumina HiSeqXten system, and 1,339,892 SNPs (Single Nucleotide Polymorphism) were generated. Filtering for < 60% missing rate and > 0.05 minor allele frequency resulted in a total of 44,255 SNPs used in GWAS. The GAPIT (Genome Association and Prediction Integrated Tool) was used to conduct based on the mean of sugar content with a Bonferroni-corrected chromosome-wide significance threshold with a -logio(P) of 5.95. The significant SNPs were obtained with fructose (seven), glucose (six), maltose (four) and sucrose (nine). There were several genes related to sugar content around the significant SNPs such as sugar transport protein 8-like, probable galactose-1 -phosphate uridyltransferase-like and beta-amylase. These results will contribute to understanding of sugar content and conversion in sweetpotato.

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Composition, the Changes of Diastase Activity and Hydroxymethylfurfural Content During Storage of the Various Honey Samples (벌꿀의 조성(組成)과 저장중(貯藏中)의 Diastase 및 Hydroxymethylfurfural함량변화(含量變化))

  • Han, Jae-Gyeong;Kim, Kwan;Kim, Dong-Youn;Lee, Sang-Kyu
    • Korean Journal of Food Science and Technology
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    • v.17 no.3
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    • pp.155-162
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    • 1985
  • The sugers and free amino acids of honey(Western and Domestic honey) and the changes of diastase activity during storage at various temperatures and HMF were studied. The average content of sugers in the western honey was 40.20% of fructose, 32.43% of glucose and 1.0% of sucrose. The average ratio of fructose to glucose was 1.24. In the case of the domestic honey, average content of sugers was 37.37% of fructose, 31.92% of glucose and 0.74% of sucrose and the average ratio of fructose to glucose was 1.19. Of the 16 amino acids detected, proline was the most predominant free amino acid in all of the honey studied, representing 39.59 to 46.86% of total free amino acids. Diastase activity of honey during the storage at $50^{\circ}C$ was rapidly decreased, but it was notably changed during storage at low temperature ($4^{\circ}C$) and room temperature ($20^{\circ}C$). The accumlated content of HMF were 0.12 to 0.47mg% during storage at 80 days at $20^{\circ}C$ and 5.35 to 8.71mg% after 3 weeks storage at $50^{\circ}C$.

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Immobilization of Kluyveromyces marxianus FO43 for Ethanol Production (Kluyveromyces marxianus FO43의 Algiante 고정화와 에탄올 발효특성)

  • Lee, Hee-Suk;Shin, Ji-Hyun;Choi, Eon-Ho
    • Applied Biological Chemistry
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    • v.38 no.1
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    • pp.20-25
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    • 1995
  • This experiment was attempted to improve ethanol productivity by immobilization of Kluyveromyces marxianus FO43 using Jerusalem artichoke powder. Sucrose medium was used to determine optimum conditions for cell immobilization. The optimum conditions were alginate concentration of 2%, bead size of 2 mm, a particle input ratio of 30 : 100, cultivation period of 24 hours, and substrate concentration of 10%(w/v). The immobilized cells produced the high concentrations of ethanol at pH $4.5{\sim}6.5$ and $30{\sim}45^{\circ}C$, broader ranges of pH and temperatures than those of free cells. Under optimum conditions the immobilized cells showed ethanol concentration of 46.4 g/L and productivity of 1.93 g/L.h. The microphotograph using a two phase contrast microscope showed that immobilized cells cultivated under the optimum conditions were densely populated toward the surface area of beads.

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Effects of oropharyngeal taste stimuli in the restoration of the fasting-induced activation of the HPA axis in rats (백서에서 금식으로 인한 스트레스 대응축 활성화의 회복조절기전에서 구강인두로부터 입수되는 다양한 맛 자극의 효과)

  • Yoo, Sang-Bae;Lee, Jong-Ho;Ryu, Vitaly;Jahng, Jeong-Won
    • Journal of the Korean Association of Oral and Maxillofacial Surgeons
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    • v.37 no.3
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    • pp.195-204
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    • 2011
  • Introduction: This study examined the regulatory mechanism underlying the meal-induced changes in the hypothalamic-pituitary-adrenal gland (HPA) axis activity. Materials and Methods: Male Sprague-Dawley rats (250-300 g) were hired for two different experiments as follows; 1) rats received either 8% sucrose or 0.2% saccharin ad libitum after 48 h of food deprivation with the gastric fistula closed (real feeding) or opened (sham feeding). 2). rats received 5 ml of intra-oral infusion with 0.2% saccharin or distilled water after 48 h of food deprivation. One hour after food access, all rats were sacrificed by a transcardiac perfusion with 4% paraformaldehyde. The brains were processed for c-Fos immunohistochemistry and the cardiac blood was collected for the plasma corticosterone assay. Results: Real feedings with sucrose or saccharin and sham feeding saccharin but not sucrose, following food deprivation decreased the plasma corticosterone level. c-Fos expression in the nucleus tractus of solitarius (NTS) of the fasted rats was increased by the consumption of sucrose but not saccharin, regardless of the feeding method. On the other hand, the consumption of sucrose or saccharin with real feeding but not the sham, induced c-Fos expression in the paraventricular nucleus (PVN) of the fasted rats. The intra-oral infusion with saccharin or water decreased the plasma corticosterone level of the fasted rats. Intra-oral water infusion increased c-Fos expression in both the PVN and NTS, but saccharin only in the NTS in the fasted rats. Conclusion: Neither restoration of the fasting-induced elevation of plasma corticosterone nor the activation of neurons in the PVN and NTS after refeeding requires the palatability of food or the post-ingestive satiety and caloric load. In addition, neuronal activation in the hypothalamic PVN may not be an implication in the restoration of the fasting-induced elevation of the plasma corticosterone by oropharyngeal stimuli of palatable food.

Protoplast Formation and Regeneration of Bacillus strains producing biopolymer (Biopolymer 생산성 Bacillus속 균주의 원형질체 형성과 재생)

  • Yim, Moo-Hyun;Kim, Seong-Ho
    • Applied Biological Chemistry
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    • v.42 no.1
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    • pp.20-28
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    • 1999
  • To improve Bacillus strains producing biopolymer, conditions for protoplast formation and regeneration were investigated in biopolymer producing Bacillus subtilis K-1 and lactose utilizing Bacillus coagulans. Bacillus subtilis K-1 mutant (SM-2) and Bacillus coagulans mutants (CM-12) were marked auxotrophic and antibiotics-resistant (SM-2) and an antibiotics-resistant mutants, respectively. To formate protoplasts derived from the mutants, conditions were established as follows. For B. subtilis mutant SM-2, its culture in mid-logarithmic phase was added with penicillin G (1.0 unit/ml) and further reacted for 1.5 hr. Cells were collected and then treated in lysis fluid (pH 7.0) containing 0.4 M sucrose and lysozyme $25\;{\mu}g/ml$ for 40 min at $37^{\circ}$. Protoplast formation was very successful (99.6%) and the ratio of cell wall regeneration was 2.4%. For Bacillus coagulans mutant CM-12, its mid-logarithmic phase culture was treated with penicillin G (0.3 unit/ml) and glycine (0.5%) for 1hr. Cells were collected and then resuspended in lysis buffer (pH 7.0) containing 0.6 M lactose and lysozyme $(300\;{\mu}g/ml)$ for 30 min at $37^{\circ}$. Protoplast formation was also successful (90.8%) and cell wall regeneration ratio was similar to SM-2 (2.2%). To improve regeneration frequency, regeneration medium was obtained as followed condition,. Cell wall regeneration was improved 2-4 folds with 5.1% for B. subtilis SM-2 and 10.3% for B. coagulans CM-12 when protoplasts mixed with soft top agar(0.4%) was overlaid onto trypticase soy broth medium containing 0.4 M sucrose, 0.7% casamino acid, 1% PVP, 25 mM $MgCl_2,\;25\;mM\;CaCl_₂$ and 1.5% agar.

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Inhibitory Effects of Wax Gourd Extract on Melanin Formation and Acne-forming Bacterial Growth (동아를 이용한 미용식품 및 화장품 개발 1. 멜라닌 생성 억제와 여드름균 억제에 미치는 동아 추출액의 효과)

  • 안용근;김승겸;신철승;민주홍
    • The Korean Journal of Food And Nutrition
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    • v.15 no.2
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    • pp.137-143
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    • 2002
  • Lyophilizate of immatured wax gourd extract was 3.1 %, matured wax gourd extract was 1.0%, and its main ingredient was sugar, which accounts for 89.7% in total residue. In matured wax gourd, pectin contents was 4.11 mg/ml, and in immatured wax gourd 4.43 mg/m1. In matured wax gourd sarcocarp, sugar contents was 0.1% of sucrose, 0.32% of glucose, 0.35% of fructose, the first unidentified sugar was 0.06% and the second was 0.04%, and all total 0.87%. In sarcocarp of immatured wax gourd, sucrose was 0.33%, glucose was 1.04%, frutcose was 1.12%, and the first unidentified sugar 0.18%, and the second was 0.l2, which total 2.79%. In matured wax gourd core, pH was 4.64, sarcocarp 4.94, immatured wax gourd core 4,96, sarcocarp 5.40. According to the organic acid analysis, in sarcocarp of matured wax gourd, citric acid of 0.409 was contained, magic acid 0.084, succnic acid 0.048%, in matured wax gourd core, citric acid was 0.648, magic acid 0.127, succinc acid 0.058%, in immatured wax gourd, citric acid 0.023, magic acid 0.219, succinic acid 0.298%, in immutured wax gourd, citric acid was 0.039, malic acid 0.350, succinic 0.224%. Fumaric acid was trace in all cases. Total organic acid in matured wax gourd core was 0.833, immatured wax gourd core was 0.624 and immatured wax gourd sarcocarp was 0.546, matured wax gourd sarcocarp was 0,541%. In inhibition rate to propionibacterium acnes, control was 0(ø, cm), wax gourd that was not heated was 2.6, and wax gourd which was heated was 2.5, concentrated by 1/5 was 1.9, wax gourd by 1/10 was 2.5, freezing dry was 2.3. Wax gourd which not heated on producing melanin in B-16 melanoma cell, the melanins forming unit was 15$\mu$1/m1 in addition of 0.01%, while that as a control was 29$\mu$1/m1.

Histidylleucine Hydrolyzing Enzyme : A Dipeptidase From Hog Lung (Dipeptidase로서의 Histidylleucine 가수분해 효소)

  • Hyun-Jae Lee;Jung-Keun Park
    • Journal of the Korean Chemical Society
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    • v.19 no.5
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    • pp.375-380
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    • 1975
  • An enzyme capable of hydrolyzing histidylleucine was purified 50 fold from hog lung. The final preparation hydrolyzed $1.6{\mu}moles$ of histidylleucime per minute per mg of protein. The $K_m$ of the enzyme for the enzyme was found to be $2{\times}10^{-4}M$. The enzyme was required a number of free dipeptides for the substrate specificity, and was inhibited by EDTA and 1,10-phenan-throline. The molecular weight of the enzyme was estimated to be 80,000 daltons from sucrose density gradient sedimentation analysis. The corrected $s_{20,w}$ value was 5.3 S.

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Role of Osmotic and Salt Stress in the Expression of Erythrose Reductase in Candida magnoliae

  • Park, Eun-Hee;Lee, Ha-Yeon;Ryu, Yeon-Woo;Seo, Jin-Ho;Kim, Myoung-Dong
    • Journal of Microbiology and Biotechnology
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    • v.21 no.10
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    • pp.1064-1068
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    • 2011
  • The osmotolerant yeast, Candida magnoliae, which was isolated from honeycomb, produces erythritol from sugars such as fructose, glucose, and sucrose. Erythrose reductase in C. magnoliae (CmER) reduces erythrose to erythritol with concomitant oxidation of NAD(P)H. Sequence analysis of the 5'-flanking region of the CmER gene indicated that one putative stress response element (STRE, 5'-AGGGG-3'), found in Saccharomyces cerevisiae, exists 72 nucleotides upstream of the translation initiation codon. An enzyme activity assay and semiquantitative reverse transcription polymerase chain reaction revealed that the expression of CmER is upregulated under osmotic and salt stress conditions caused by a high concentration of sugar, KCl, and NaCl. However, CmER was not affected by osmotic and oxidative stress induced by sorbitol and $H_2O_2$, respectively. The basal transcript level of CmER in the presence of sucrose was higher than that in cells treated with fructose and glucose, indicating that the response of CmER to sugar stress is different from that of GRE3 in S. cerevisiae, which expresses aldose reductase in a sugarindependent manner. It was concluded that regulation of CmER differs from that of other aldose reductases in S. cerevisiae.