Cellulose degradation in Glenea cantor (Fabricius) (Coleoptera: Cerambycidae): functional characterization of GcEGaseZ7 and Cellulase reveals a novel enzymatic activity.

IF 2.1 3区 农林科学 Q1 ENTOMOLOGY Journal of Insect Science Pub Date : 2024-11-01 DOI:10.1093/jisesa/ieae101
Ran-Ran Su, Tai-Hui Lan, Bi-Qiong Pan, Xia-Lin Zheng, Wen Lu, Xiao-Yun Wang
{"title":"Cellulose degradation in Glenea cantor (Fabricius) (Coleoptera: Cerambycidae): functional characterization of GcEGaseZ7 and Cellulase reveals a novel enzymatic activity.","authors":"Ran-Ran Su, Tai-Hui Lan, Bi-Qiong Pan, Xia-Lin Zheng, Wen Lu, Xiao-Yun Wang","doi":"10.1093/jisesa/ieae101","DOIUrl":null,"url":null,"abstract":"<p><p>Glenea cantor (Fabricius) is an important forest pest that mainly attacks kapok trees, breaking down cellulose and lignin through 3 enzyme activities: endoglucanase, filter paper enzyme, and cellobiase. In this study, we unveiled the cloning and expression of 10 endoglucanase genes, GcEGase5A1, GcEGase5A2, GcEGaseZ2, GcEGaseZ3, GcEGaseZ4, GcEGaseZ5, GcEGaseZ7, GcEGaseZ8, GcEGaseZ9, and Cellulase, all of which exhibit enzymatic activities in G. cantor. These findings indicated that Cellulase shares sequence homology with beetle GHF45, whereas the other 9 endoglucanase genes are homologous to beetle GHF5. GcEGaseZ4 presented the highest expression in the foregut. In contrast, GcEGase5A2 and Cellulase presented peak expression in the midgut. Furthermore, GcEGaseZ7 was identified as the most highly expressed endoglucanase in the hindgut. Functional assays confirmed the ability of GcEGaseZ7 and Cellulase to degrade cellulose, and their cellulase activities were 75.57 ± 1.21 U/mg and 344.79 ± 6.91 U/mg, respectively. These results enhance our understanding of the complex cellulase system in insects and provide insights into the efficient digestion of cellulosic materials by wood-consuming insects. This research also has potential applications in bioenergy production and the development of biomaterials from lignocellulosic biomass.</p>","PeriodicalId":16156,"journal":{"name":"Journal of Insect Science","volume":"24 6","pages":""},"PeriodicalIF":2.1000,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11583219/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Insect Science","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1093/jisesa/ieae101","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"ENTOMOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Glenea cantor (Fabricius) is an important forest pest that mainly attacks kapok trees, breaking down cellulose and lignin through 3 enzyme activities: endoglucanase, filter paper enzyme, and cellobiase. In this study, we unveiled the cloning and expression of 10 endoglucanase genes, GcEGase5A1, GcEGase5A2, GcEGaseZ2, GcEGaseZ3, GcEGaseZ4, GcEGaseZ5, GcEGaseZ7, GcEGaseZ8, GcEGaseZ9, and Cellulase, all of which exhibit enzymatic activities in G. cantor. These findings indicated that Cellulase shares sequence homology with beetle GHF45, whereas the other 9 endoglucanase genes are homologous to beetle GHF5. GcEGaseZ4 presented the highest expression in the foregut. In contrast, GcEGase5A2 and Cellulase presented peak expression in the midgut. Furthermore, GcEGaseZ7 was identified as the most highly expressed endoglucanase in the hindgut. Functional assays confirmed the ability of GcEGaseZ7 and Cellulase to degrade cellulose, and their cellulase activities were 75.57 ± 1.21 U/mg and 344.79 ± 6.91 U/mg, respectively. These results enhance our understanding of the complex cellulase system in insects and provide insights into the efficient digestion of cellulosic materials by wood-consuming insects. This research also has potential applications in bioenergy production and the development of biomaterials from lignocellulosic biomass.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Glenea cantor (Fabricius) (Coleoptera: Cerambycidae) 的纤维素降解:GcEGaseZ7 和纤维素酶的功能特性揭示了一种新型酶活性。
木棉虫(Glenea cantor)是一种重要的森林害虫,主要侵害木棉树,通过内切葡聚糖酶、滤纸酶和纤维生物酶三种酶的活性分解纤维素和木质素。本研究揭示了10个内切葡聚糖酶基因的克隆和表达,包括GcEGase5A1、GcEGase5A2、GcEGaseZ2、GcEGaseZ3、GcEGaseZ4、GcEGaseZ5、GcEGaseZ7、GcEGaseZ8、GcEGaseZ9和纤维素酶,这些基因在坎特蝇中都具有酶活性。这些发现表明,纤维素酶与甲虫 GHF45 具有序列同源性,而其他 9 个内切葡聚糖酶基因与甲虫 GHF5 具有同源性。GcEGaseZ4 在前肠的表达量最高。相比之下,GcEGase5A2 和纤维素酶在中肠的表达量最高。此外,GcEGaseZ7 被确定为后肠中表达量最高的内切葡聚糖酶。功能测试证实了 GcEGaseZ7 和纤维素酶降解纤维素的能力,它们的纤维素酶活性分别为 75.57 ± 1.21 U/mg 和 344.79 ± 6.91 U/mg 。这些结果加深了我们对昆虫复杂纤维素酶系统的了解,并为木材消耗昆虫高效消化纤维素材料提供了启示。这项研究还可能应用于生物能源生产和木质纤维素生物质生物材料的开发。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Journal of Insect Science
Journal of Insect Science 生物-昆虫学
CiteScore
3.70
自引率
0.00%
发文量
80
审稿时长
7.5 months
期刊介绍: The Journal of Insect Science was founded with support from the University of Arizona library in 2001 by Dr. Henry Hagedorn, who served as editor-in-chief until his death in January 2014. The Entomological Society of America was very pleased to add the Journal of Insect Science to its publishing portfolio in 2014. The fully open access journal publishes papers in all aspects of the biology of insects and other arthropods from the molecular to the ecological, and their agricultural and medical impact.
期刊最新文献
Bee cups 2.0: P-cups as single-use cages for honey bee (Hymenoptera: Apidae) experiments. Direct and indirect effects of selective insecticides on 2 generalist predators of Bemisia tabaci (Hemiptera: Aleyrodidae). Low-density migratory beekeeping induces intermediate disturbance effects on native bee communities in Tibetan Plateau alpine meadows. Population records reveal expanded habitat preference for the endemic, predaceous Jamaican fungus gnat Neoditomyia farri (Diptera, Keroplatidae). Cellulose degradation in Glenea cantor (Fabricius) (Coleoptera: Cerambycidae): functional characterization of GcEGaseZ7 and Cellulase reveals a novel enzymatic activity.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1