Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill].

Abstract:

:The enzymatic properties of novel cysteine proteases D3-alpha and beta which were purified from germinating soybean cotyledons were investigated. The enzyme activities were exhibited in the presence of a thiol reagent, such as 2-mercaptoethanol, and apparently inhibited by E-64, a cysteine protease inhibitor. Hydrolytic activities toward carbobenzoxy-Phe-Arg-MCA were detected at a pH above 4.0. The optimum temperature for activities was about 40 degrees C. The isoelectric point of D3-alpha and beta was 4.4 and 4. 7, respectively. The molecular mass of D3-alpha and beta, measured by MALDI/TOF mass spectrometry, was 26,178 and 26,429 Da, respectively. The substrate specificities of the enzymes were examined using peptide-MCAs and peptides, and cathepsin L-like broad specificity was observed at pH 4.0. These results demonstrated that these enzymes are cysteine endopeptidases [EC 3.4.22.-] like papain [EC 3.4.22.2].

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Asano M,Suzuki S,Kawai M,Miwa T,Shibai H

doi

10.1093/oxfordjournals.jbchem.a022448

keywords:

subject

Has Abstract

pub_date

1999-08-01 00:00:00

pages

296-301

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

126

pub_type

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