Purification and characterization of a chloride ion-dependent α-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis)
Purification and characterization of a chloride ion-dependent α-glucosidase from the midgut gland of Japanese scallop (Patinopecten yessoensis)
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日本扇贝（虾夷扇贝）中肠腺氯离子依赖性 α-葡萄糖苷酶的纯化和表征
DOI：
10.1080/09168451.2015.1116926
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
Mori H & Kimura A
中科院分区：
文献类型：
--
作者：
Masuda Y;Okuyama M;Iizuka T;Nakai H;Saburi W;Fukukawa T;Maneesan J;Tagami T;Naraoka T;Mori H & Kimura A
海洋糖苷水解酶因其与生境相关的特性，如耐作为盐性、耐压性和耐冷性，而具有巨大的应用潜力。从虾夷扇贝（Patinopecten yessoensis）中肠腺中分离纯化了一种α-葡萄糖苷酶（PYG），发现该酶具有独特的性质。在纯化过程中使用阿卡波糖亲和层析特别有效，使比活性增加570倍。PYG是一种有趣的氯离子依赖性酶。氯离子导致其酶性质发生显著变化，增加其水解速率，改变其酶活性的pH值分布，将其pH稳定性范围转移到碱性区域，并将其最佳温度从37 ° C提高到55 °C。此外，氯离子改变PYG的底物特异性。PYG在无氯离子存在下对麦芽八糖的Vmax/Km值最高，在有氯离子存在下对麦芽三糖的Vmax/Km值最高。
Marine glycoside hydrolases hold enormous potential due to their habitat-related characteristics such as salt tolerance, barophilicity, and cold tolerance. We purified an α-glucosidase (PYG) from the midgut gland of the Japanese scallop (Patinopecten yessoensis) and found that this enzyme has unique characteristics. The use of acarbose affinity chromatography during the purification was particularly effective, increasing the specific activity 570-fold. PYG is an interesting chloride ion-dependent enzyme. Chloride ion causes distinctive changes in its enzymatic properties, increasing its hydrolysis rate, changing the pH profile of its enzyme activity, shifting the range of its pH stability to the alkaline region, and raising its optimal temperature from 37 to 55 °C. Furthermore, chloride ion altered PYG’s substrate specificity. PYG exhibited the highestVmax/Kmvalue toward maltooctaose in the absence of chloride ion and toward maltotriose in the presence of chloride ion.