Aminopeptidase GX, and a method of hydrolyzing a protein with the same
First Claim
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1. A purified aminopeptidase GX derived from germinated soybean cotyledon having the following properties:
- a) optimum pH occurs in the range;
about 5.5 to about 9.5;
b) optimum temperature occurs in the range;
about 25°
to about 60°
C.;
c) temperature stability;
about 80% or more activity remains after being kept at 50°
C. for 80 minutes or about 40% or more activity remains after being kept at 60°
C. for 40 minutes;
d) molecular weight;
about 400 to 550 kD (gel filtration),about 380 to 460 kD (native PAGE), and three subunits ofabout 53 to 60 kD, about 30 to 32 kD,and about 25 to 28 kD (SDS-PAGE afterreduction and heating);
e) substrate specificity;
decomposes a peptide or protein containing glutamic acid or aspartic acid at the N-terminus to release the glutamic acid or aspartic acid;
f) inhibitors;
inhibited by leuhistin, actinonin, alphamenine A or 1,10-orthophenanthroline; and
g) effect of metal ions;
inhibited by magnesium or copper.
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Abstract
An aminopeptidase is provided which efficiently decomposes a low-molecular-weight peptide containing glutamic acid or aspartic acid in its sequence. A method of hydrolyzing a peptide or protein by use of the aminopeptidase is also provided. Aminopeptidase GX is derived from germinated soybean cotyledons and releases glutamic acid or aspartic acid from a peptide or protein containing glutamic acid or aspartic acid at the N-terminal end and is used to hydrolyse peptides or proteins.
6 Citations
5 Claims
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1. A purified aminopeptidase GX derived from germinated soybean cotyledon having the following properties:
-
a) optimum pH occurs in the range;
about 5.5 to about 9.5;b) optimum temperature occurs in the range;
about 25°
to about 60°
C.;c) temperature stability;
about 80% or more activity remains after being kept at 50°
C. for 80 minutes or about 40% or more activity remains after being kept at 60°
C. for 40 minutes;d) molecular weight;
about 400 to 550 kD (gel filtration),about 380 to 460 kD (native PAGE), and three subunits of about 53 to 60 kD, about 30 to 32 kD, and about 25 to 28 kD (SDS-PAGE after reduction and heating); e) substrate specificity;
decomposes a peptide or protein containing glutamic acid or aspartic acid at the N-terminus to release the glutamic acid or aspartic acid;f) inhibitors;
inhibited by leuhistin, actinonin, alphamenine A or 1,10-orthophenanthroline; andg) effect of metal ions;
inhibited by magnesium or copper. - View Dependent Claims (2, 3, 4, 5)
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Specification
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Current AssigneeAjinomoto Co., Inc.
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Original AssigneeAjinomoto Co., Inc.
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InventorsKawai, Misako, Nio, Noriki, Miwa, Tetsuya, Asano, Minao
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Primary Examiner(s)Grimes, Eric
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Assistant Examiner(s)Tung, Peter P.
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Application NumberUS08/813,591Time in Patent Office592 DaysField of Search435/212, 435/68.1, 435/106, 435/109, 435/110US Class Current435/212CPC Class CodesC12N 9/48 acting on peptide bonds (3.4)
