NDLI: Fructo-oligosaccharide synthesis by mutant versions of Saccharomyces cerevisiae invertase.

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Fructo-oligosaccharide synthesis by mutant versions of Saccharomyces cerevisiae invertase.

Content Provider	Semantic Scholar
Author	Lafraya, Alvaro Aguado Sanz-Aparicio, Julia Polaina, Julio Marín-Navarro, Julia
Copyright Year	2011
Abstract	Efficient enzymatic synthesis of tailor-made prebiotic fructo-oligosaccharides (FOS) used in functional food formulation is a relevant biotechnological objective. We have engineered the Saccharomyces cerevisiae invertase (Suc2) to improve its transferase activity and to identify the enzymatic determinants for product specificity. Amino acid replacement (W19Y, N21S, N24S) within a conserved motif (β-fructosidase) specifically increased the synthesis of 6-kestose up to 10-fold. Mutants with lower substrate (sucrose) affinity produced FOS with longer half-lives. A mutation (P205V) adjacent to another conserved motif (EC) caused a 6-fold increment in 6-kestose yield. Docking studies with a Suc2 modeled structure defined a putative acceptor substrate binding subsite constituted by Trp 291 and Asn 228. Mutagenesis studies confirmed the implication of Asn 228 in directing the orientation of the sucrose molecule for the specific synthesis of β(2,6) linkages.
Starting Page	365
Ending Page	375
Page Count	11
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://aem.asm.org/content/77/17/6148.full.pdf
PubMed reference number	21764973v1
Alternate Webpage(s)	https://doi.org/10.1128/AEM.05032-11
DOI	10.1128/aem.05032-11
Journal	Applied and environmental microbiology
Volume Number	77
Issue Number	17
Language	English
Access Restriction	Open
Subject Keyword	6-kestose Amino Acids Asparagine Functional Food Invertase Mutation Polyisoprenyl Phosphate Oligosaccharides Prebiotics Protein Domain Saccharomyces cerevisiae Sucrose Transferase Version oligosaccharide biosynthetic process
Content Type	Text
Resource Type	Article

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