Molecular characterization of β-fructofuranosidases from Rhizopus delemar and Amylomyces rouxii
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- DNA, Fungal chemistry genetics MeSH
- Phylogeny MeSH
- Hydrolysis MeSH
- beta-Fructofuranosidase genetics isolation & purification metabolism MeSH
- Molecular Sequence Data MeSH
- Mucorales enzymology genetics MeSH
- Oligosaccharides metabolism MeSH
- Polymerase Chain Reaction MeSH
- Sucrose metabolism MeSH
- Sequence Analysis, DNA MeSH
- Sequence Homology, Amino Acid MeSH
- Cluster Analysis MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- DNA, Fungal MeSH
- fructooligosaccharide MeSH Browser
- beta-Fructofuranosidase MeSH
- Oligosaccharides MeSH
- Sucrose MeSH
Of the 19 strains of Rhizopus delemar deposited as Rhizopus oryzae, seven of them, NBRC 4726, NBRC 4734, NBRC 4746, NBRC 4754, NBRC 4773, NBRC 4775, and NBRC 4801, completely hydrolyzed exogenous sucrose and fructooligosaccharides. The sucrose-hydrolyzing enzyme was purified from the culture filtrate of R. delemar NBRC 4754 and classified to β-fructofuranosidase, similar to that of Amylomyces rouxii CBS 438.76. Fragments including β-fructofuranosidase genes (sucA) of seven strains of R. delemar and A. rouxii CBS 438.76 were amplified and sequenced by PCR with degenerated primers synthesized on the basis of the internal amino acid sequences of purified enzymes and successive inverse PCR. Nucleotide sequences of the obtained fragments revealed that open reading frames of 1,569 bp have no intron and encode 522 amino acids. The presumed proteins contained the typical domain of the glycoside hydrolase 32 family, including β-fructofuranosidase, inulinase, levanase, and fructosyltransferases. Amino acid sequences of SucA proteins from the seven strains of R. delemar were identical and showed 90.0 % identity with those of A. rouxii CBS 438.76. A dendrogram constructed from these amino acid sequences showed that SucA proteins are more closely related to yeast β-fructofuranosidases than to other fungal enzymes.
See more in PubMed
Mycologia. 2007 Sep-Oct;99(5):714-22 PubMed
Indian J Biochem Biophys. 2001 Jun;38(3):180-5 PubMed
Appl Microbiol Biotechnol. 1995 Dec;44(1-2):47-52 PubMed
Mikrobiologiia. 2011 Jul-Aug;80(4):496-507 PubMed
Gene. 2011 Sep 15;484(1-2):26-34 PubMed
J Ind Microbiol Biotechnol. 2008 Nov;35(11):1253-9 PubMed
Biotechnol Adv. 2009 Mar-Apr;27(2):145-52 PubMed
Enzyme Microb Technol. 1991 Jun;13(6):495-8 PubMed
Recent Pat Food Nutr Agric. 2009 Nov;1(3):221-30 PubMed
Comput Appl Biosci. 1996 Aug;12(4):357-8 PubMed
Arch Microbiol. 2004 Sep;182(1):30-6 PubMed
BMC Genomics. 2011 Jan 17;12:38 PubMed
Biosci Biotechnol Biochem. 2009 Apr 23;73(4):861-4 PubMed
FEMS Yeast Res. 2002 Jan;1(4):247-56 PubMed
J Physiol Biochem. 2009 Sep;65(3):315-28 PubMed
Curr Genet. 1989 Sep;16(3):145-52 PubMed
J Bras Pneumol. 2010 Jan-Feb;36(1):134-41 PubMed
Nucleic Acids Res. 2009 Jan;37(Database issue):D233-8 PubMed
J Biosci Bioeng. 2002;94(1):78-80 PubMed
J Ind Microbiol Biotechnol. 2010 Nov;37(11):1137-43 PubMed
Appl Microbiol Biotechnol. 2008 Mar;78(3):379-89 PubMed
Annu Rev Microbiol. 1983;37:575-601 PubMed
Nucleic Acids Res. 1994 Nov 11;22(22):4673-80 PubMed
Biosci Biotechnol Biochem. 2008 Dec;72(12):3167-73 PubMed
GENBANK
AB701479, AB701480, AB701481, AB701482