Purification and Properties of Two Proteolytic Enzymes with Carboxypeptidase Activity in Germinated Wheat | Zendy

K.R. Preston | Zendy; James E. Kruger | Zendy

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Purification and Properties of Two Proteolytic Enzymes with Carboxypeptidase Activity in Germinated Wheat

Author(s) -

K.R. Preston,

James E. Kruger

Publication year - 1976

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.58.4.516

Subject(s) - carboxypeptidase , enzyme , biochemistry , proteolytic enzymes , gluten , hydrolysis , chemistry , germination , hemoglobin , proline , amino acid , enzymatic hydrolysis , food science , biology , botany

Two proteolytic enzymes with carboxypeptidase activity have been isolated from a germinated wheat extract and partially characterized. Both enzymes rapidly released amino acids from hemoglobin and gluten and hydrolyzed carbobenzoxy-phenylalanylalanine. The enzymes were inhibited by diisopropylphosphofluoridate, but unaffected by salts, ethylenediaminetetraacetate, and sulfhydryl reagents at lower concentrations, and had molecular weights of approximately 55,000 and 61,000. Analysis of the hydrolysis products of hemoglobin and gluten indicated that both enzymes had broad specificities, including the ability to release proline.

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