|
KMID : 1134819960250040687
|
|
Journal of the Korean Society of Food Science and Nutrition
1996 Volume.25 No. 4 p.687 ~ p.694
|
|
|
Purification and Enzymatic Properties of Myrosinase in Korean Mustard Seed(Brassica juncea)
|
|
Shin Chang-Sik
Seo Kwon-Il
Kang Kap-Suk
Ahn Cheol-Woo
Kim Yong-Gwan
Shim Ki-Hwan
|
|
|
Abstract
|
|
|
|
Myrosinase was purified from Korean mustard seed(Brassica juncea) by a sequential process of DEAE-cellulose, concanavalin A-sepharose, and Superose 6 chromatography. The molecular weight of puri-fied myrosinase(Ⅱ-2) determined by SDS-polyacrylamide electrophoresis was 67KD. About a 248-fold purification for myrosinase Ⅱ-2 was obtained after Superose 6 chromatography. Optimum pH of the myrosinase was 7.0 and optimum temperature of the enzyme was 37℃. The enzyme was stable at pH 7.0, and below 30℃. Cu, Hg and Fe ion significantly inhibited the enzyme activity, but ascorbic acid enhanced, resulting in a maximum activity by 1mM ascorbic acid. Among the ascorbic acid ana-logues, dehydroascorbic acid inhibited the enzyme activity, whereas others showed a little effect. Reducing agents such as 2-mercaptoethanol and dithiothreitol inhibited the enzyme activity, but the reducing agents with ascorbic acid was enhanced enzyme activity.
|
|
|
KEYWORD
|
|
|
mustard seed, myrosinase, purification, enzymatic property
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
|