Circular Dichroism Analysis of MRJP2 Purified from Royal Jelly

doi:10.7506/spkx1002-6630-201323013

Abstract

Abstract:

MRJP2, a member of the major royal jelly protein (MRJP) family, was extracted from fresh royal jelly, purified
by affinity chromatography, molecular sieve chromatography and ion exchange chromatography and identified by SDSPAGE
and mass spectrum. The MRJP protein was analyzed by synchrotron radiation circular dichroism (SRCD) to clarify
its secondary structure as a function of temperature, pH and ion concentrations. The results of this study showed that heat treatment
at elevated temperatures from 10 to 90 ℃ resulted in increased proportion of α-helix and decreased proportion of β-strand
and random coil, while the proportion of β-turn kept stable. As the pH varied from 4.0 to 9.0, the proportion of α-helix revealed
an initial decrease followed by an increase, the highest proportions of β-strand and random coil were found at pH 5.0 and 8.0,
respectively, and the proportion of β-turn remained basically unchanged. After different metal ions were added in the protein
solution, the proportion of α-helix was increased by Ca2+ but decreased by Mg2+ and Zn2+.

Key words: royal jelly, MRJP2, purification, secondary structure, circular dichroism (CD)

CLC Number:

TS201.2

HU Yi-fan1,2，CHEN Zhong-zhou2，TIAN Wen-li1,2，ZHAO Ya-zhou1，PENG Wen-jun1,*. Circular Dichroism Analysis of MRJP2 Purified from Royal Jelly[J]. FOOD SCIENCE, 2013, 34(23): 57-61.

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