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The starch-binding domains (SBDs) are structurally and functionally independent non-catalytic protein module widely found in carbohydrate active enzymes (CAZymes), and they play an important role in the degradation process of raw starch in ecological environment. In nature, SBDs effectively lead the catalytic domain to the substrate surface by specifically binding to starch granules or other polysaccharides, significantly enhancing the hydrolytic efficiency of enzymes. In addition to the non-hydrolytic disruptive activity on the structure of starch granules, SBDs widely influence many catalytic properties of host enzymes, including substrate specificity, environmental adaptability (thermostability, salt tolerance, and cold adaptation), and oligomerization state. These roles demonstrate their adaptive function in helping host microorganisms to compete for carbon sources in complex habitats. Here, we summarized the distribution characteristics, functional mechanisms, and multiple effects of SBDs on host enzyme functions in terrestrial and marine ecosystems. The main experimental methods for studying SBD functions, including domain deletion, functional characterization of binding and disruption, are also introduced. A broader and deeper understanding of SBDs enhances our knowledge of microbial competition for carbon sources in natural environments, as well as provides novel approaches for the rational design of industrial enzymes.

, authors=Hui PENG^*, Zi-jian FU, authorsList=Hui PENG, Zi-jian FU, authorCompany=null, correspAuthors=Hui PENG, authorNote=null, correspAuthorsNote=null, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=null, magXml=null, pdfUrl=null, pdf=null, pdfFileSize=null, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=null, mapNumber=null, fund=null), CN=ArticleExt(id=1315696650400674227, articleId=1315696649939300784, tenantId=1146029695717560320, journalId=1315121759093096577, language=CN, title=淀粉结合结构域（SBD）在微生物环境适应与碳源竞争中的多功能角色, columnId=1315696196023333441, journalTitle=微生物学杂志, columnName=大家专版, runingTitle=null, highlight=null, articleAbstract=

淀粉结合结构域（Starch-binding domain, SBD）广泛分布于碳水化合物活性酶（CAZymes）的末端，是一个独立的非催化的结构域，也是淀粉颗粒自然降解过程中的重要功能模块。自然界中，SBD可以特异性识别并结合淀粉颗粒或其他多糖，然后将酶的催化结构域引导到糖类物质的表面，显著提高了酶的水解效率。SBD能以非水解的方式破坏淀粉颗粒的结构，还能广泛影响酶的多种催化特性，包括底物特异性、环境适应性（如热稳定性、耐盐性与适冷性）和寡聚化状态等。对SBD生理生化功能的深入研究有助于理解微生物在复杂生境中如何竞争碳源和适应环境。本文综述了SBD在陆地和海洋生态系统中的分布情况、SBD与底物的作用机制以及SBD对宿主酶不同功能的影响。此外，总结了SBD功能的研究方法，包括结构域缺失、结合与破坏能力表征等技术。对SBD的深入研究，不仅拓宽了对自然界中微生物碳源竞争方式的认知，也为工业酶理性设计提供了新的改造思路。

, authors=彭惠^*, 付自建, authorsList=彭惠, 付自建, authorCompany=null, correspAuthors=彭惠, authorNote=, correspAuthorsNote=, copyrightStatement=null, copyrightOwner=null, extLink=null, articleAbsUrl=null, sourceXml=3iUzypPsHQGeAzsxsg5P6w==, magXml=/FUMmnL+lhT4XHKNSPxWnA==, pdfUrl=null, pdf=GEh7Xu1o3d2hjgNkYtNppw==, pdfFileSize=1471492, pdfExtLink=null, richHtmlUrl=null, mobilePdfUrl=null, reviewReport=null, pdfFirstPage=null, abstractGraph=null, abstractGraphContent=null, abstractVideo=null, citation=null, cebUrl=null, magXmlContent=r728WXJGuYJpUpYc17xy/w==, mapNumber=null, fund=null)}, authors=[Author(id=1315696650677498296, tenantId=1146029695717560320, journalId=1315121759093096577, articleId=1315696649939300784, orderNo=0, firstName=null, middleName=null, lastName=null, nameCn=null, orcid=null, stid=null, country=null, authorPic=null, dead=0, email=penghui@ahu.edu.cn, emailSecond=null, emailThird=null, correspondingAuthor=1, authorType=1, ext={EN=AuthorExt(id=1315696650761384378, tenantId=1146029695717560320, journalId=1315121759093096577, articleId=1315696649939300784, authorId=1315696650677498296, language=EN, stringName=Hui PENG, firstName=Hui, middleName=null, lastName=PENG, prefix=null, suffix=null, authorComment=null, nameInitials=null, affiliation=null, department=null, xref=^*, address=School of Life Sciences and Medical Engineering, Anhui University, Hefei 230601, bio=null, bioImg=null, bioContent=null, aboutCorrespAuthor=null), CN=AuthorExt(id=1315696650832687547, tenantId=1146029695717560320, journalId=1315121759093096577, articleId=1315696649939300784, authorId=1315696650677498296, language=CN, stringName=彭惠, firstName=null, middleName=null, lastName=null, prefix=null, suffix=null, authorComment=null, nameInitials=null, affiliation=null, department=null, xref=^*, address=安徽大学 生命科学与医学工程学院，安徽 合肥　230601, bio={"content":"

彭惠　女，教授，博士，博士生导师。研究方向为生物催化与微生物。Tel: 0551-63861928，E-mail: penghui@ahu.edu.cn

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彭惠　女，教授，博士，博士生导师。研究方向为生物催化与微生物。Tel: 0551-63861928，E-mail: penghui@ahu.edu.cn

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