Details

Autor(en) / Beteiligte

• Yuan, Bo
• Hu, Nan
• Sun, Juan
• Wang, Shi-An
• Li, Fu-Li

Titel

Purification and characterization of a novel extracellular inulinase from a new yeast species Candida kutaonensis sp. nov. KRF[1.sup.T]

Ist Teil von

• Applied microbiology and biotechnology, 2012-12, Vol.96 (6), p.1517

Ort / Verlag

Springer

Erscheinungsjahr

2012

Quelle

2022 ECC(Springer)

Beschreibungen/Notizen

• A novel extracellular exoinulinase was purified and characterized from a new yeast strain [KRF1.sup.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.sub.m] and [V.sub.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°C, and the enzyme remained 78 % of activity at 60°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.sup.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.sup.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.sup.T] =AS [2.4027.sup.T]=CBS [11388.sup.T]) is proposed.