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Assignment of the disulfide bonds in the sweet protein brazzein

✍ Scribed by Masanori Kohmura; Masafumi Ota; Hiroyuki Izawa; Ding Göran Ming Hellekant; Yasuo Ariyoshi

Publisher
Wiley (John Wiley & Sons)
Year
1998
Tongue
English
Weight
249 KB
Volume
38
Category
Article
ISSN
0006-3525

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✦ Synopsis

The thermostable sweet protein brazzein consists of 54 amino acid residues and has four intrumolecular disulfide bonds, the location qf which is unknown. We found that bruzzein resists enzymatic hydrol-vsis at enzyme/substrute ratios ( w / w ) of 1:100-1:10 at 35-40°C for 24-48 h. Brazzein wus hjdrolyzed using thermolysin at an enzyme/.substrute ratio ofl:I ( w / w ) in water, p H 5.5,,fi,r 6 h and U I 50°C. The disuljide bonds were determined, by a combination ($muss spectrometric unulysis und amino acid sequencing ofc.vstine-containing peptides, to be between Cys4-Cy.sS2, Cys16-Cys37, C)~.s22-Cys47, and Cys26-Cys49. These disulfide bonds contribute to its thermostability.

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