Results 161 to 170 of about 1,207 (175)

Cruciferin coating improves the stability of chitosan nanoparticles at low pH

Journal of Materials Chemistry B, 2016
Encapsulation is an emerging technique to improve the solubility, permeability and bioavailability of bioactive compounds.
Ali, Akbari, Jianping, Wu
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Molecular analysis of a cruciferin storage protein gene family of Brassica napus

Plant Molecular Biology, 1992
We have isolated a five-member gene subfamily which encodes cruciferin, a legumin-like 12S storage protein of Brassica napus L., and have analyzed the structure and expression of the family members in developing embryos. Sequence analysis has shown that the coding regions of all five genes are highly similar, with the two most divergent members of the ...
J P, Breen, M L, Crouch
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Preliminary Crystallographic Analysis of a Cruciferin Protein from Seeds of Moringa oleifera

The Protein Journal, 2014
A 55 kDa cruciferin protein has been purified and characterized from seeds of Moringa oleifera plant. Protein blast of N-terminal amino-acid sequence showed 60 % sequence similarity with cruciferin from Brassica napus. The M. oleifera protein has been crystallized applying the sitting drop method using 5 % polyethylene glycol 8,000, 38.5 % 3-methyl-1,5-
Ahmed, Akrem, Nasser, Yousef, Afshan, Begum, Amr, Negm, Arne, Meyer, Markus, Perbandt, Friedrich, Buck, Christian, Betzel   +7 more
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Comparison of Protein Chemical and Physicochemical Properties of Rapeseed Cruciferin with Those of Soybean Glycinin

Journal of Agricultural and Food Chemistry, 2002
Rapeseeds contain cruciferin (11S globulin), napin (2S albumin), and oleosin (oil body protein) as major seed proteins. The effects of oil expression and drying conditions on the extraction of these proteins from rapeseed meal were examined. The conditions strongly affected the extraction of oleosin and only weakly affected the extraction of cruciferin
Mohamad Ramlan Bin, Mohamed Salleh, Nobuyuki, Maruyama, Motoyasu, Adachi, Naho, Hontani, Shiori, Saka, Noboru, Kato, Yasunobu, Ohkawa, Shigeru, Utsumi   +7 more
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Isolation and functional characterization of the Brassica napus cruciferin gene cru4 promoter

Journal of the Korean Society for Applied Biological Chemistry, 2014
The 12S globulin protein cruciferin is main seed storage protein in Brassica napus. To gain a better understanding of the Bncru4 promoter function, we conducted the promoter 5′ deletion analysis in transgenic Arabidopsis. In the β-glucuronidase (GUS) expression assay, Bncru4 promoter was strongly active in transgenic seeds.
Kyung Hee Roh, Soo Bok Choi, Han-Chul Kang, Jong-Bum Kim, Hyun Uk Kim, Kyeong-Ryeol Lee, Sun Hee Kim   +6 more
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THE EFFECT OF pH ON RAPESEED GLOBULIN (CRUCIFERIN) BINDING TO ANILINONAPHTHALENE-8-SULFONATE

Journal of Food Biochemistry, 1995
The fluorescence emission intensity from rapeseed globulin (cruciferin) increased in the presence of anilinonaphthalene-8-sulfonate (ANS) at pH 2.0 but not at pH 10. Fluorescence titration studies showed that at pH 7 cruciferin binds 22 (±0.6) moles of ANS per mole of protein with an average dissociation constant (K d ) of 1.9 (±0.1) x 10 -5 M.
RICHARD K. OWUSU APENTEN, YETUNDE L. FOLAWIYO   +1 more
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Polyelectrolyte Complex Nanoparticles from Chitosan and Acylated Rapeseed Cruciferin Protein for Curcumin Delivery

Journal of Agricultural and Food Chemistry, 2018
Curcumin is a polyphenol that exhibits several biological activities, but its low aqueous solubility results in low bioavailability. To improve curcumin bioavailability, this study has focused on developing a polyelectrolyte complexation method to form layer-by-layer assembled nanoparticles, for curcumin delivery, with positively charged chitosan (CS ...
Fengzhang Wang, Yijie Yang, Xingrong Ju, Chibuike C. Udenigwe, Rong He   +4 more
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The Effect of pH and NaCl Levels on the Physicochemical and Emulsifying Properties of a Cruciferin Protein Isolate

Food Biophysics, 2013
The influence of pH (3.0, 5.0, and 7.0) and ionic strength (0, 50, 100 mM NaCl) on the physicochemical and emulsifying properties of a cruciferin-rich protein isolate (CPI) was investigated. Surface charge on the CPI was found to substantially reduced in the presence of NaCl.
Lamlam Cheung, Janitha Wanasundara, Michael T. Nickerson   +2 more
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Proteomic identification of allergenic seed proteins, napin and cruciferin, from cold-pressed rapeseed oils

Food Chemistry, 2015
In Finland and France atopic children commonly react to seeds of oilseed rape and turnip rape in skin prick tests (SPT) and open food challenges. These seeds are not as such in dietary use and therefore the routes of sensitization are unknown. Possible allergens were extracted from commercial cold-pressed and refined rapeseed oils and identified by gel-
Puumalainen, T. J., Puustinen, A., Poikonen, S., Turjanmaa, K., Palosuo, T., Vaali, K.   +5 more
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Solubility, Heat-Induced Gelation and Pepsin Susceptibility of Cruciferin Protein as Affected by Subunit Composition

Food Biophysics, 2014
This study examined the solubility, heat-induced gel formation ability, and pepsin susceptibility of cruciferin with mixed (wild type, WT) or identical subunits (CRUA, CRUB, or CRUC). All cruciferin species exhibited minimal solubility at pH 4.0 and slight solubility between pH 7.5 and 8, which was not influenced by the presence of NaCl.
Thushan S. Withana-Gamage, Dwayne D. Hegedus, Xiao Qiu, Janitha Wanasundara   +3 more
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