Grosch W, Laskaway G, Kaiser K P
Z Lebensm Unters Forsch. 1977 Nov 25;165(2):77-81. doi: 10.1007/BF02427785.
Isolation and purification of soya bean lipoxygenase (linoleate: O2 oxidoreductase, EC, 1.13.11.12) on Sephadex G-200, DEAE-cellulose and by isolectric focusing yields two isoenzymes of the L- 2 type (optimum pH 6.5) and two of the L-1 type (optimum pH9.0). Different crude extracts from soya beans as well as the purified L-2 isoenzymes exhibit the same capacity for co-oxidation of beta-carotene and canthaxanthine, when the comparison is based upon equal lipoxygenase activities. In contrast to L-2 the alkaline lipoxygenase L-1 is a poor "carotene oxidase".
利用葡聚糖G - 200、二乙氨基乙基纤维素并通过等电聚焦法对大豆脂氧合酶(亚油酸:O₂氧化还原酶,EC 1.13.11.12)进行分离和纯化,得到了两种L - 2型同工酶(最适pH 6.5)和两种L - 1型同工酶(最适pH 9.0)。当基于相等的脂氧合酶活性进行比较时,来自大豆的不同粗提物以及纯化的L - 2同工酶对β - 胡萝卜素和角黄素的共氧化表现出相同的能力。与L - 2相反,碱性脂氧合酶L - 1是一种较差的“胡萝卜素氧化酶”。