A protease/peptidase from culture medium of Flammulina velutipes that acts on arabinogalactan-protein
A protease/peptidase from culture medium of Flammulina velutipes that acts on arabinogalactan-protein
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来自金针菇培养基的作用于阿拉伯半乳聚糖蛋白的蛋白酶/肽酶
DOI：
10.1080/09168451.2016.1258985
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
--
作者：
Yoshimi;Y.;Sugawara;Y.;Hori;C.;Igarashi;K.;Kaneko;S.;Tsumuraya;Y.;and Kotake;T.
阿拉伯半乳聚糖蛋白（AGPs）是在植物细胞表面发现的高度多样的植物蛋白聚糖。AGP具有大的阿拉伯半乳聚糖（AG）部分，其连接至富含羟脯氨酸（Hyp）的核心蛋白。AG通过各种糖苷水解酶进行水解，其中大部分已经被鉴定，而核心蛋白可能被自然界中真菌和细菌分泌的未知蛋白酶/肽酶降解。虽然已知几种水解其他富含Hyp-rich蛋白的酶，但作用于AGP核心蛋白的酶仍有待鉴定。本研究描述了对AGP核心蛋白的蛋白酶/肽酶活性的检测在培养基中的冬菇（金针菇）和部分纯化的酶的几个常规的色谱步骤。该酶对羟脯氨酸残基比对脯氨酸和丙氨酸残基表现出更高的活性，并作用于从阿拉伯树胶制备的核心蛋白。由于在Pefabloc SC存在下活性受到抑制，因此该酶可能是丝氨酸蛋白酶。
Arabinogalactan-proteins (AGPs) are highly diverse plant proteoglycans found on the plant cell surface. AGPs have large arabinogalactan (AG) moieties attached to a core-protein rich in hydroxyproline (Hyp). The AG undergoes hydrolysis by various glycoside hydrolases, most of which have been identified, whereas the core-proteins is presumably degraded by unknown proteases/peptidases secreted from fungi and bacteria in nature. Although several enzymes hydrolyzing other Hyp-rich proteins are known, the enzymes acting on the core-proteins of AGPs remain to be identified. The present study describes the detection of protease/peptidase activity toward AGP core-proteins in the culture medium of winter mushroom (Flammulina velutipes) and partial purification of the enzyme by several conventional chromatography steps. The enzyme showed higher activity toward Hyp residues than toward proline and alanine residues and acted on core-proteins prepared from gum arabic. Since the activity was inhibited in the presence of Pefabloc SC, the enzyme is probably a serine protease.