23
DOI: https://doi.org/10.1016/j.jgeb.2024.100402
English
eng
Tran Dinh Minh
Contributor
<p><span style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;"><span style="margin: 0px; padding: 0px;"><a href="https://www.sciencedirect.com/topics/pharmacology-toxicology-and-pharmaceutical-science/bacilli" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">Bacillus</a></span><em style="margin: 0px; padding: 0px;"> velezensis</em></span><span style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;"> RB.IBE29 harbors two <a href="https://www.sciencedirect.com/topics/pharmacology-toxicology-and-pharmaceutical-science/chitinase" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">chitinases</a><span style="margin: 0px; padding: 0px;"> belonging to the <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/glycoside-hydrolase" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">glycoside hydrolase</a><span style="margin: 0px; padding: 0px;"><span style="margin: 0px; padding: 0px;"> family 18 and exhibiting a novel domain structure. The roles of these <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/chitinase" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">chitinases</a> in crop production have been reported; nevertheless, their contribution to controlling </span><a href="https://www.sciencedirect.com/topics/immunology-and-microbiology/human-pathogen" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">human pathogens</a> is unknown. In this initial work, the chitinases A (BvChiA) and B (BvChiB) of strain RB.IBE29 were produced in recombinant </span></span></span><em style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;">Escherichia coli</em><span style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;"> BL21-CodonPlus (DE3)-RIPL cells and subsequently purified using HisTrap FF column. The purified BvChiA and BvChiB exhibited the highest chitinase and <a href="https://www.sciencedirect.com/topics/immunology-and-microbiology/binding-affinity" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">binding activities</a><span style="margin: 0px; padding: 0px;"><span style="margin: 0px; padding: 0px;"> against colloidal <a href="https://www.sciencedirect.com/topics/pharmacology-toxicology-and-pharmaceutical-science/chitin" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">chitin</a>. Combining both chitinases for the </span><a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/enzymatic-hydrolysis" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">hydrolysis</a><span style="margin: 0px; padding: 0px;"> of powdered <a href="https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/chitin" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">chitin</a> increased the reducing sugar content by 88.7 %. Moreover, the purified chitinases remarkably suppressed the germination of </span></span></span><span style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;"><span style="margin: 0px; padding: 0px;"><a href="https://www.sciencedirect.com/topics/immunology-and-microbiology/candida-albicans" class="topic-link" style="margin: 0px; padding: 0px; background-color: rgba(0, 0, 0, 0); word-break: break-word; text-decoration: underline 1px rgb(31, 31, 31); color: rgb(31, 31, 31); text-underline-offset: 1px;">Candida albicans</a></span></span><span style="color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;"> VTCC 20568 (=JCM 2070) cells. These results indicated that the novel domain-structure-containing chitinases of strain RB.IBE29 have great potential and can be further developed as a novel therapeutic agent against human pathogenic </span><em style="margin: 0px; padding: 0px; color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;">C. albicans</em><span style="color: rgb(31, 31, 31); font-family: ElsevierGulliver, Georgia, "Times New Roman", Times, STIXGeneral, "Cambria Math", "Lucida Sans Unicode", "Microsoft Sans Serif", "Segoe UI Symbol", "Arial Unicode MS", serif, sans-serif; font-size: 16px;">.</span></p>
Elsevier
September 2024
pdf
Journal of Genetic Engineering and Biotechnology
Novel domain-structure-containing chitinases A and B of Bacillus velezensis produced by recombinant Escherichia coli cells: Synergism on chitin degradation and their potential in suppressing Candida albicans cell germination
mixed material
Elsevier