Preparation of low-molecular-weight citrus pectin by recombinant Bacillus subtilis pectate lyase and promotion of growth of Bifidobacterium longum

2018 ◽  
Vol 107 ◽  
pp. 39-42 ◽  
Author(s):  
Ming-qi Liu ◽  
Wen-kang Huo ◽  
XianJun Dai ◽  
Ya-hui Dang
2019 ◽  
Vol 7 (4) ◽  
pp. 108
Author(s):  
Yeo Ok Han ◽  
Yunju Jeong ◽  
Hyun Ju You ◽  
Seockmo Ku ◽  
Geun Eog Ji ◽  
...  

Rotavirus infection is the most common diarrheal disease worldwide in children under five years of age, and it often results in death. In recent years, research on the relationship between rotavirus and probiotics has shown that probiotics are effective against diarrhea. A clinical trial has reported that Bifidobacterium longum BORI reduced diarrhea induced by rotavirus. The present work investigated the anti-rotaviral effect of B. longum BORI by cytopathic effect observation and real time cell analyses. Our study found that B. longum BORI showed strong anti-rotaviral effect when incubated with MA104 cells prior to viral infection, suggesting that the probiotic does in fact interfere with the interaction of viruses and host cells. It is believed that the efficacy is due to low-molecular weight and non-protein components derived from B. longum BORI. This discovery can help broaden the industrial application of B. longum BORI, which has been proven to be a safe and effective probiotic.


2004 ◽  
Vol 51 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Kazuo Miyairi ◽  
Ai Ogasawara ◽  
Akio Tonouchi ◽  
Kouzou Hosaka ◽  
Makiko Kudou ◽  
...  

2005 ◽  
Vol 187 (14) ◽  
pp. 4945-4956 ◽  
Author(s):  
Lucia Musumeci ◽  
Cristina Bongiorni ◽  
Lutz Tautz ◽  
Robert A. Edwards ◽  
Andrei Osterman ◽  
...  

ABSTRACT In gram-negative organisms, enzymes belonging to the low-molecular-weight protein tyrosine phosphatase (LMPTP) family are involved in the regulation of important physiological functions, including stress resistance and synthesis of the polysaccharide capsule. LMPTPs have been identified also in gram-positive bacteria, but their functions in these organisms are presently unknown. We cloned two putative LMPTPs from Bacillus subtilis, YfkJ and YwlE, which are highly similar to each other in primary structure as well as to LMPTPs from gram-negative bacteria. When purified from overexpressing Escherichia coli strains, both enzymes were able to dephosphorylate p-nitrophenyl-phosphate and phosphotyrosine-containing substrates in vitro but showed significant differences in kinetic parameters and sensitivity to inhibitors. Transcriptional analyses showed that yfkJ was transcribed at a low level throughout the growth cycle and underwent a σB-dependent transcriptional upregulation in response to ethanol stress. The transcription of ywlE was growth dependent but stress insensitive. Genomic deletion of each phosphatase-encoding gene led to a phenotype of reduced bacterial resistance to ethanol stress, which was more marked in the ywlE deletion strain. Our study suggests that YfkJ and YwlE play roles in B. subtilis stress resistance.


2019 ◽  
Vol 59 (10) ◽  
pp. 1004-1015 ◽  
Author(s):  
Bassem M. Salama ◽  
Wafaa A. Helmy ◽  
Tamer I. M. Ragab ◽  
Mamdouh M. Ali ◽  
Hanan A. A. Taie ◽  
...  

2006 ◽  
Vol 188 (4) ◽  
pp. 1509-1517 ◽  
Author(s):  
Huimin Xu ◽  
Bin Xia ◽  
Changwen Jin

ABSTRACT The low-molecular-weight (LMW) protein tyrosine phosphatases (PTPs) exist ubiquitously in prokaryotes and eukaryotes and play important roles in cellular processes. We report here the solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis. YwlE consists of a twisted central four-stranded parallel β-sheet with seven α-helices packing on both sides. Similar to LMW PTPs from other organisms, the conformation of the YwlE active site is favorable for phosphotyrosine binding, indicating that it may share a common catalytic mechanism in the hydrolysis of phosphate on tyrosine residue in proteins. Though the overall structure resembles that of the eukaryotic LMW PTPs, significant differences were observed around the active site. Residue Asp115 is likely interacting with residue Arg13 through electrostatic interaction or hydrogen bond interaction to stabilize the conformation of the active cavity, which may be a unique character of bacterial LMW PTPs. Residues in the loop region from Phe40 to Thr48 forming a wall of the active cavity are more flexible than those in other regions. Ala41 and Gly45 are located near the active cavity and form a noncharged surface around it. These unique properties demonstrate that this loop may be involved in interaction with specific substrates. In addition, the results from spin relaxation experiments elucidate further insights into the mobility of the active site. The solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial LMW PTPs.


2008 ◽  
Vol 190 (17) ◽  
pp. 5738-5745 ◽  
Author(s):  
Sumarin Soonsanga ◽  
Jin-Won Lee ◽  
John D. Helmann

ABSTRACTOhrR proteins can be divided into two groups based on their inactivation mechanism: 1-Cys (represented byBacillus subtilisOhrR) and 2-Cys (represented byXanthomonas campestrisOhrR). A conserved cysteine residue near the amino terminus is present in both groups of proteins and is initially oxidized to the sulfenic acid. TheB. subtilis1-Cys OhrR protein is subsequently inactivated by formation of a mixed-disulfide bond with low-molecular-weight thiols or by cysteine overoxidation to sulfinic and sulfonic acids. In contrast, theX. campestris2-Cys OhrR is inactivated when the initially oxidized cysteine sulfenate forms an intersubunit disulfide bond with a second Cys residue from the other subunit of the protein dimer. Here, we demonstrate that the 1-CysB. subtilisOhrR can be converted into a 2-Cys OhrR by introducing another cysteine residue in either position 120 or position 124. Like theX. campestrisOhrR protein, these mutants (G120C and Q124C) are inactivated by intermolecular disulfide bond formation. Analysis of oxidized 2-Cys variants both in vivo and in vitro indicates that intersubunit disulfide bond formation can occur simultaneously at both active sites in the protein dimer. Rapid formation of intersubunit disulfide bonds protects OhrR against irreversible overoxidation in the presence of strong oxidants much more efficiently than do the endogenous low-molecular-weight thiols.


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