Characterization of cyanogenic β-glucosidase (Linamarase) from cassava (Manihot esculenta Crantz)

• Main Authors: Thidarat Eksittikul, Montri Chulavatnatol
• Other Authors: Mahidol University
• Format: Article
• Published: 2018
• Subjects: Biochemistry, Genetics and Molecular Biology
• Online Access: https://repository.li.mahidol.ac.th/handle/123456789/15498

Linamarase (EC 3.2.1.21) was purified from cassava petiole, stem, and root cortex by ammonium sulfate precipitation, column chromatography on Sepharose 6B, and chromatofocusing. The last step resolved the enzyme from each source into three forms with pI values of 4.3, 3.3, and 2.9. Each form was found to be oligomeric, consisting of one kind of subunit, M r 63,000. The major isozyme with a pI of 4.3 from petiole showed a K m for linamarin of 0.6 mm and possessed both β-glucosidase and β-fucosidase activities. The former was sensitive to inhibition by δ-gluconolactone, isopropyl-β-d-thioglucoside, and HgCl 2 , whereas the latter was inhibited by Tris ion. © 1988.