Isolation and characterization of the K5-type yeast killer protein and its homology with an exo-beta-1,3-glucanase

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2004-03-01
Izgu, F
Altinbay, D
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K5-type yeast killer protein in the culture supernatant of Pichia anomala NCYC 434 cells was concentrated by ultrafiltration and purified to homogenity by ion-exchange chromatography with a POROS HQ/M column followed by gel filtration with a TSK G2000SW column. The protein migrated as a single band on discontinous gradient SDS-PAGE and had a molecular mass of 49000 Da. The pI value of the K5-type killer protein was measured at pH 3.7 by high voltage vertical gel electrofocusing. The result of an enzyme immuno assay revealed that it was a glycosylated protein. Its internal amino acid sequencing yielded the sequences LNDFWQQGYHNL, IPIGYWAFQLLDNDPY, and YGGSDYGDVVIGIELL, which are 100% identical to exo-beta-1,3-glucanase (accession no. AJ222862) of Pichia anomala (strain K). The purified protein was highly stable at pH values between 3 and 5.5 and temperatures up to 37degreesC.
Biotechnology, Organic Chemistry, Analytical Chemistry, Applied Microbiology and Biotechnology, Biochemistry, Molecular Biology, General Medicine
https://hdl.handle.net/11511/65670
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Department of Biology, Article

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Citation Formats
F. Izgu and D. Altinbay, “Isolation and characterization of the K5-type yeast killer protein and its homology with an exo-beta-1,3-glucanase,” BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, pp. 685–693, 2004, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/65670.
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