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Nakamura, Soichiro,Ogawa, Masahiro,Saeki, Hiroki,Saito, Masayoshi,Miyasaka, Satoko,Hata, Junya,Adachi, Naoko,Hwang, Jae-Kwan The Korean Society of Food Science and Nutrition 2000 Preventive Nutrition and Food Science Vol.5 No.4
Protein conjugation of curdlan belonging to $\beta$-1, 3-glucan was carried out to improve it surface functionalities. The glucan was mixed with phosvitin, {TEX}$$\alpha$_{s}${/TEX}-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and he resulting powder was incubated at 6$0^{\circ}C$ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. conjugation with unfolding proteins, i.e., phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbmin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the {TEX}$$\alpha$_{s}${/TEX}-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
Soichiro Nakamura,Masahiro Ogawa,Hiroki Saeki,Masayoshi Saito,Satoko Miyasaka,Junya Hata,Naoko Adachi,Jae-Kwan Hwang 한국식품영양과학회 2000 Preventive Nutrition and Food Science Vol.5 No.4
Protein conjugation of curdlan belonging to β-1,3-glucan was carried out to improve its surface functionalities. The glucan was mixed with phosvitin, α_s-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and the resulting powder was incubated at 60℃ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. Conjugation with unfolding proteins, i.e., phosvitin and α_s-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbumin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the α_s-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and α_s-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
Washida, Haruhiko,Sugino, Aya,Kaneko, Sachiyo,Crofts, Naoko,Sakulsingharoj, Chotipa,Kim, Dongwook,Choi, Sang-Bong,Hamada, Shigeki,Ogawa, Masahiro,Wang, Changlin,Esen, Asim,Higgins, Thomas J.V.,Okita, Blackwell Publishing Ltd 2009 The Plant journal Vol.60 No.1
<P>Summary</P><P>The RNAs for the storage proteins of rice (<I>Oryza sativa</I>), prolamines and glutelins, which are stored as inclusions in the lumen of the endoplasmic reticulum (ER) and storage vacuoles, respectively, are targeted by specific <I>cis</I>-localization elements to distinct subdomains of the cortical ER. Glutelin RNA has one or more <I>cis</I>-localization elements (zip codes) at the 3′ end of the RNA, whereas prolamine has two <I>cis</I>-elements; one located in the 5′ end of the coding sequence and a second residing in the 3′-untranslated region (UTR). We had earlier demonstrated that the RNAs for the maize zeins (‘prolamine’ class) are localized to the spherical protein body ER (PB-ER) in developing maize endosperm. As the PB-ER localization of the 10-kDa &dgr;-zein RNA is maintained in developing rice seeds, we determined the number and proximate location of their <I>cis</I>-localization elements by expressing GFP fusions containing various zein RNA sequences in transgenic rice and analyzing their spatial distribution on the cortical ER by <I>in situ</I> RT-PCR and confocal microscopy. Four putative <I>cis</I>-localization elements were identified; three in the coding sequences and one in the 3′-UTR. Two of these zip codes are required for restricted localization to the PB-ER. Using RNA targeting determinants we show, by mis-targeting the storage protein RNAs from their normal destination on the cortical ER, that the coded proteins are redirected from their normal site of deposition. Targeting of RNA to distinct cortical ER subdomains may be the underlying basis for the variable use of the ER lumen or storage vacuole as the final storage deposition site of storage proteins among flowering plant species.</P>