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Article

Structural features and activity of Brazzein and its mutants upon substitution of a surfaced exposed alanine.

Biochimie - 1 Dec 2016

Ghanavatian Parisa, Khalifeh Khosrow, Jafarian Vahab

Abstract excerpt

Brazzein (Brz) is a member of sweet-tasting protein containing four disulfide bonds. It was reported as a compact and heat-resistant protein. Here, we have used site-directed mutagenesis and replaced a surface-exposed alanine with aspartic acid (A19D mutant), lysine (A19K mutant) and glycine (A19G mutant). Activity comparisons of wild-type (WT) and mutants using taste panel test procedure showed that A19G variant...

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Source

Identifiers

PMID: 27616457
DOI: 10.1016/j.biochi.2016.09.006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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