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

Issued Date

1988-01-01

Resource Type

Article

ISSN

10960384
00039861

DOI

10.1016/0003-9861(88)90257-3

Other identifier(s)

2-s2.0-0024095252

Rights

Mahidol University

Rights Holder(s)

SCOPUS

Bibliographic Citation

Archives of Biochemistry and Biophysics. Vol.266, No.1 (1988), 263-269

Suggested Citation

Thidarat Eksittikul, Montri Chulavatnatol Characterization of cyanogenic β-glucosidase (Linamarase) from cassava (Manihot esculenta Crantz). Archives of Biochemistry and Biophysics. Vol.266, No.1 (1988), 263-269. doi:10.1016/0003-9861(88)90257-3 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/15498

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Title

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

Author(s)

Thidarat Eksittikul
 Montri Chulavatnatol

Other Contributor(s)

Mahidol University

Abstract

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.

Keyword(s)

Biochemistry, Genetics and Molecular Biology

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https://repository.li.mahidol.ac.th/handle/20.500.14594/15498

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