نتایج جستجو برای: chitin binding domain

تعداد نتایج: 765299  

ژورنال: :پژوهش های سلولی و ملکولی 0
سهیلا مطرودی تهران، پژوهشگاه ملی مهندسی ژنتیک و زیست فناوری خرمشهر، دانشگاه علوم و فنون دریایی خرمشهر محمدرضا زمانی تهران، پژوهشگاه ملی مهندسی ژنتیک و زیست فناوری مصطفی مطلبی تهران، پژوهشگاه ملی مهندسی ژنتیک و زیست فناوری

آنزیم¬های کایمری از جمله پروتئین¬های مهندسی شده می¬باشند که از تغییر در ساختار آنزیم¬ها بدست می¬آیند. آنزیم¬های کیتینازی بدلیل توانایی در تجزیه ترکیبات کیتینی، در تولید پروتوپلاست قارچی، تبدیل زیستی shellfish waste به بخش های تک جزئی، تولید الیگوساکاریدها و کنترل قارچ¬های بیماریزا حائز اهمیت می-باشند. در این تحقیق پس از تکثیر ناحیه (chitin binding domain) chbd کیتینازb باکتری serratia marcescen...

Journal: Mycologia Iranica 2016

Evidence for the role of chitinases in biocontrol by Trichoderma species has been well documented.Chit42 lacks a chitin–binding domain (ChBD) which is involved in its binding activity to insoluble chitin. The objective of the present study was to enhance antifungal activity of T. harzianum by overexpression of wild type and hybrid forms of Chit42 containing chitin binding domain. To produce chi...

ژورنال: :مجله پژوهش های سلولی و مولکولی 2015
سهیلا مطرودی محمدرضا زمانی مصطفی مطلبی

آنزیم¬های کایمری از جمله پروتئین¬های مهندسی شده می¬باشند که از تغییر در ساختار آنزیم¬ها بدست می¬آیند. آنزیم¬های کیتینازی بدلیل توانایی در تجزیه ترکیبات کیتینی، در تولید پروتوپلاست قارچی، تبدیل زیستی shellfish waste به بخش های تک جزئی، تولید الیگوساکاریدها و کنترل قارچ¬های بیماریزا حائز اهمیت می-باشند. در این تحقیق پس از تکثیر ناحیه (chitin binding domain) chbd کیتینازb باکتری serratia marcescen...

Journal: :iranian journal of biotechnology 2015
thu ngoc le thi huyen do thanh nhan nguyen ngoc tan tran sven olof enfors

background: enterocin-p of enterococcus faecium p13 (entp) is of great interest as a food preservative and medicine due to its non-toxicity and broad antimicrobial spectrum in various ph, as well as its excellent thermal stability. however, recombinant production of entp is still in laboratory because of low productivity and complex purification process. objectives: in this study, we aimed to d...

Journal: :Microbiology 1998
A L Svitil D L Kirchman

To examine the ecology and evolution of microbial chitinases, especially the chitin-binding domain, one of the chitinase genes (chiA) from the marine bacterium Vibrio harveyi was analysed. The deduced amino acid sequence of ChiA is not very similar overall to other proteins, except for two regions, the putative catalytic and chitin-binding domains. Among all bacterial chitinases sequenced to da...

2013
Andrea Sánchez-Vallet Raspudin Saleem-Batcha Anja Kombrink Guido Hansen Dirk-Jan Valkenburg Bart PHJ Thomma Jeroen R Mesters

While host immune receptors detect pathogen-associated molecular patterns to activate immunity, pathogens attempt to deregulate host immunity through secreted effectors. Fungi employ LysM effectors to prevent recognition of cell wall-derived chitin by host immune receptors, although the mechanism to compete for chitin binding remained unclear. Structural analysis of the LysM effector Ecp6 of th...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2000
D M van Aalten B Synstad M B Brurberg E Hough B W Riise V G Eijsink R K Wierenga

In this paper, we describe the structure of chitinase B from Serratia marcescens, which consists of a catalytic domain with a TIM-barrel fold and a 49-residue C-terminal chitin-binding domain. This chitinase is the first structure of a bacterial exochitinase, and it represents one of only a few examples of a glycosyl hydrolase structure having interacting catalytic and substrate-binding domains...

Journal: :Journal of microbiology and biotechnology 2009
Chien-Jui Huang Shu-Huei Guo Shu-Chun Chung Yu-Ju Lin Chao-Ying Chen

An antifungal chitinase, ChiCW, produced by Bacillus cereus 28-9 is effective against conidial germination of Botrytis elliptica, the causal agent of lily leaf blight. ChiCW as a modular enzyme consists of a signal peptide, a catalytic domain, a fibronectin type-III-like domain, and a chitin-binding domain. When two C-terminal domains of ChiCW were truncated, ChiCWdeltaFC (lacking the chitin-bi...

Journal: :Protein science : a publication of the Protein Society 2011
Marylène Vandevenne Vincent Campisi Astrid Freichels Carole Gillard Gilles Gaspard Jean-Marie Frère Moreno Galleni Patrice Filée

This work analyses the chitin-binding and catalytic domains of the human macrophage chitotriosidase and investigates the physiological role of this glycoside hydrolase in a complex mechanism such as the innate immune system, especially its antifungal activity. Accordingly, we first analyzed the ability of its chitin-binding domain to interact with chitin embedded in fungal cell walls using the ...

2016
Firas Fadel Yuguang Zhao Alexandra Cousido-Siah Francesc X. Ruiz André Mitschler Alberto Podjarny

Chitinases are enzymes that catalyze the hydrolysis of chitin. Human chitotriosidase (CHIT1) is one of the two active human chitinases, involved in the innate immune response and highly expressed in a variety of diseases. CHIT1 is composed of a catalytic domain linked by a hinge to its chitin binding domain (ChBD). This latter domain belongs to the carbohydrate-binding module family 14 (CBM14 f...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید