Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 96, Issue 6, Pages 1517-1526Publisher
SPRINGER
DOI: 10.1007/s00253-012-4108-y
Keywords
Candida kutaonensis sp nov.; Conserved motif; Inulinase; Purification; Yeast
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Funding
- National Natural Science Foundation of China (NSFC) [30900007]
- Chinese Academy of Sciences [KSCX2-EW-J-10]
- China Agriculture Research System [CARS-35]
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A novel extracellular exoinulinase was purified and characterized from a new yeast strain KRF1(T), and the gene encoding the enzyme was successfully cloned. The enzyme was stable at low pH between 3.0 and 6.5. The K (m) and V (max) values of the purified enzyme for inulin were 2.3 mg/mL and 4.8 mg/min, respectively. The optimum temperature of the inulinase was 50 A degrees C, and the enzyme remained 78 % of activity at 60 A degrees C for 2 h. The inulinase showed an amino acid sequence identity of 58 % to its closest homolog in Meyerozyma (Pichia) guilliermondii. In the secondary structure, the domain G (VMEVH) of the enzyme contained three unique residues (V, M, and H). Compared with previously reported inulinases, the enzyme from strain KRF1(T) displayed strong acid resistance, notable thermostability, and high affinity for the substrate of inulin. Based on sequence analysis of the 26S rDNA D1/D2 domain and phenotypic characterization, the yeast strain KRF1(T) was found to represent a novel anamorphic, ascomycetous yeast species. A complete description of the species is given and the name Candida kutaonensis sp. nov (type strain = KRF1(T) = AS 2.4027(T) = CBS 11388(T)) is proposed.
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