Liu Junhua, Dai Mei, Li Jiangtao, Zhang Yitong, Ren Yangjie, Xu Jichen, Gao Wei, Guo Sujuan
Biological Physics Laboratory, College of Science, Beijing Forestry University, Beijing, China.
National Engineering Laboratory of Tree Breeding, Beijing Forestry University, Beijing, China.
Front Bioeng Biotechnol. 2022 Apr 5;10:870672. doi: 10.3389/fbioe.2022.870672. eCollection 2022.
Dehydrins (DHNs) belong to group II of late embryogenesis-abundant (LEA) proteins, which are up-regulated in most plants during cold, drought, heat, or salinity stress. Despite the importance of dehydrins for the plants to resist abiotic stresses, it is necessary to obtain plant-derived dehydrins from different biomass. Generally, dehydrin PicW1 from is involved in Kn-type dehydrin with five K-segments, which has a variety of biological activities. In this work, dehydrin PicW1 was expressed in and purified by chitin-affinity chromatography and size-exclusion chromatography, which showed as a single band by SDS-PAGE. A cold-sensitive enzyme of lactate dehydrogenase (LDH) is used to explore the protective activities of other proteins. Temperature stress assays showed that PicW1 had an effective protective effect on LDH activity, which was better than that of bovine serum albumin (BSA). This study provides insights into the purification and protective activity of K5 DHNs for the advancement of dehydrin structure and function from biomass.
脱水素（DHNs）属于胚胎发育晚期丰富蛋白（LEA）的第二组，在大多数植物受到寒冷、干旱、高温或盐胁迫时会上调表达。尽管脱水素对植物抵抗非生物胁迫很重要，但有必要从不同生物质中获取植物来源的脱水素。一般来说，来自[具体来源未给出]的脱水素PicW1属于具有五个K片段的Kn型脱水素，具有多种生物学活性。在这项工作中，脱水素PicW1在[具体表达宿主未给出]中表达，并通过几丁质亲和层析和尺寸排阻层析进行纯化，在SDS-PAGE上显示为单一条带。一种对温度敏感的乳酸脱氢酶（LDH）被用于探究其他蛋白质的保护活性。温度胁迫试验表明，PicW1对LDH活性具有有效的保护作用，优于牛血清白蛋白（BSA）。这项研究为从生物质中推进脱水素结构和功能的K5 DHNs的纯化和保护活性提供了见解。
