• Title/Summary/Keyword: Korean native-bee honey

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Discrimination of Native Bee-Honey and Foreign Bee-Honey by SDS-PAGE (단백질 전기영동을 이용한 토종꿀의 판별)

  • Lee, Deug-Chan;Lee, Sang-Young;Cha, Sang-Hoon;Choi, Yong-Soon;Rhee, Hae-Ik
    • Korean Journal of Food Science and Technology
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    • v.30 no.1
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    • pp.1-5
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    • 1998
  • To find out the difference between native bee-honey (NBH) and foreign bee-honey (FBH), quantification of honey protein and investigation of specific protein in NBH were carried out by SDS-PAGE. Contents of honey protein in NBH and FBH were measured by Bradford and Lowry method. The contents of protein determined by Bradford method were $0.1{\sim}3.3\;mg/g$ in NBH and $0.2{\sim}1.6\;mg/g$ in FBH, and by Lowry method were $12.9{\sim}45.7\;mg/g$ in NBH and $15.8{\sim}27.1\;mg/g$ in FBH. In order to investigate the distribution of bee honey proteins, the SDS-PAGE was performed. The results showed that molecular weight of the major proteins in NBH and in FBH were 56 kDa and 59 kDa. respectively. Therefore, it was confirmed that the difference between NBH and FBH can be identified visually by SDS-PAGE analysis. The major proteins in NBH and FBH were purified through two step chromatography, and the obtained proteins were used as marker protein in SDS-PAGE to discriminate NBH and FBH.

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Minerals, HMF and Vitamins of Honey Harvested in Kangwon Area (강원도산 벌꿀의 무기물 , HMF 및 비타민에 관한 연구)

  • 김복남;김택제;최홍식
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.23 no.4
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    • pp.675-679
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    • 1994
  • Minerals, hydroxymethyfufural (HMF) and vitamins in native bee-honey (NBH) harvested from four different areas of Kangwon, korea were analyzed . Ash content of NBH varied from 0.26 to 0.50 % with the mean and standard deviation values of 0.32$\pm$ 0.17% and those of FBH varied from 0.15 to 0.58%(0.32$\pm$0.37) . Among analyzed minerals, the concentration of K,Ca, Mg, Fe and P except Na in NBH were found to be higher than those in FBH. The amounts of K and NA in NBH were 1200-3200ppm(2000 $\pm$770ppm) and 35-50ppm(38$\pm$6ppm), and those in FBH were 1100-3300ppm(1900$\pm$ 1700ppm) and 32-72ppm(49$\pm$17ppm), respectively. The mean value of Na to K ratio expressed as Na/Kx10$^3$ was 20$\pm$4 for the NBH and 41$\pm$25 for the FBH. HMF levels in NBH were 0.50$\pm$0.22mg% which was twice as much as those in FBH. Ascorbic acid and riboflavin in NBH were present at the range of 2.2-4.0mg% and 0.17-0.24mg% , respectively, of which were not significantly different from those obtained from the FBH.

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A Study on Analysis of Residual Antibiotics and Prop Acid in Honey (벌꿀중의 잔유항생물질 및 Propionic Acid 분석011 관한 조사연구)

  • 전상수
    • Journal of environmental and Sanitary engineering
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    • v.5 no.2
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    • pp.63-80
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    • 1990
  • A sensitive and simple analytical system for the simultaneous determination of residual oxytetracycline, tetracycline, and doxycycline in honey was described, and that the analytical method for determination of residual propionic acid in honey was established. Experimental subjects were purchased four kinds of honey, native kind honey, acaccia honey, mixed floral honey, chestnut honey in Kyung Sang Nam Do. Several microbiological methods are available to determine tetracycline antibiotecs(TCs) in foods but their precision apears to be variable and the specificity is questionable. These methods are considered to be not suitable for analysis of tetracycline antibiotics in honey because honey itself has bacteriostatic action. For determination of tetracycline antibiotics in honey, therefore the High Performance Liquid Chromatography(HPLC) method was applied, and the propionic acid were determined by Gas Chromatography(5.C). Ethylacetate, as an extract solvent, was found to be suitable for seperation of TCs in honey, but methanol and acetone were not. The recoverly rate of Oxytetracycline(OTC), Tetracycline(TC), Doxycycline(DC) from honey spiked at a level of 10 $\mu $g/g were 97%, 89%, and 91%, respectively. The cailbration curve in TCs was linear expression from 2$\mu $g/ml to 10$\mu $g/ml. As the results of analysis, the residual tetracycline antibiotics were not detected in the 100 samples of honey. The recovery rate of propionic acid from honey spiked at level of 10$\mu $g/g was 98.3% , and the calibra lion curves were linear expression from 21$\mu $g/ml to 101$\mu $g/ml. As the results of analysis, the residual propionic acid was not detected in the 100 samples of honey. Retention time(min) of OTC, DC, and TC were 3.35, 4.61, and 5.30 minutes at the conditions of table 2, respectively, and retention time(min) of propionic acid was 3.50 minutes at the conditions of table 3. The residual TCs and propionic acid were not detected in the 100 samples of honey, but there is a possibility that antibiotics or propionic acid will be to remain in honey if they are used during product period in order to prevent putrefaction of honey-bee.

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Isolation and Characterization of Major Royal Jelly cDNAs and Proteins of the Honey Bee (Apis cerana)

  • Srisuparbh, Duangporn;Klinbunga, Sirawut;Wongsiri, Siriwat;Sittipraneed, Siriporn
    • BMB Reports
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    • v.36 no.6
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    • pp.572-579
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    • 2003
  • An expressed sequence tag (EST) library was established from the hypopharyngeal glands of Apis cerana. Sixty-six recombinant clones, possessing inserts >500 bp, were randomly selected and unidirectional sequenced. Forty-two of these (63.6%) were identified as homologues of Major Royal Jelly Proteins families 1, 2, 3, and 4 of A. mellifera (AmMRJP) for which MRJP1 was the most abundant family. The open-reading frame of the MRJP1 homologue (AcMRJP1) was 1299 nucleotides that encoded 433 deduced amino acids with three predicted N-linked glycosylation sites. The AcMRJP1 sequence showed 93% and 90% homologies with nucleotide and deduced amino acid sequences of AmMRJP1, respectively. Two complete transcripts of apisimin, and one and two partial transcripts of $\alpha$-glucosidase and glucose oxidase, were also isolated. In addition, the royal jelly proteins of A. cerana were purified and characterized using Q-Sepharose and Sephadex G-200 column chromatography. The native forms of protein peaks A1, A2, B1, and C1 were 115, 55, 50, and 300 kDa, respectively. SDS-PAGE analysis indicated that A1 and C1 were dimeric and oligomeric forms of the 80 kDa and 50 kDa subunits, respectively. The ratio of the total protein quantities of A1 : A2 : B1 : C1 were 2.52 : 4.72 : 1 : 12.21. Further characterization of each protein, using N-terminal and internal peptide sequencing, revealed that the respective proteins were homologues of MRJP3, MRJP2, MRJP1, and MRJP1 of A. mellifera.