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Killer toxin of Pichia anomala NCYC 432; purification, characterization and its exo-β-1,3-glucanase activity

Paper ID Volume ID Publish Year Pages File Format Full-Text
18504 42725 2006 8 PDF Available
Title
Killer toxin of Pichia anomala NCYC 432; purification, characterization and its exo-β-1,3-glucanase activity
Abstract

Pichia anomala NCYC 432 secretes a killer toxin which is inhibitory to a variety of yeasts including pathogenic Candida spp. The killer toxin in the culture supernatant was concentrated by ultrafiltration and purified to homogenity by two successive gel filtration chromatographies with a TSK G2000SW column. Biochemical characterization of the toxin showed that it is a glycosylated protein with a molecular mass of 47 kDa and pI values of 3.4 and 3.7. The toxin showed high stability at pH values between 3 and 5.5 and up to 37 °C. Its N-terminal amino acid sequencing yielded the sequence GDYWDYQNDKIR which is 100% identical with that of mature exo-β-1,3-glucanase (accession no. AJ222862) of P. anomala strain K. The toxin displayed high activity against laminarin thus showing a β-glucanase activity. The Michaelis constants Km and Vmax for laminarin hydrolysis were 0.3 mg ml−1 and 350 μmol min−1 mg−1.

Keywords
Killer yeast; Pichia anomala; Killer toxin; exo-β-1,3-Glucanase
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Killer toxin of Pichia anomala NCYC 432; purification, characterization and its exo-β-1,3-glucanase activity
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 39, Issue 4, 2 August 2006, Pages 669–676
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us