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
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Bifidobacterium Longum ◽  
Pectate Lyase ◽  
Low Molecular Weight ◽  
Citrus Pectin ◽  
Recombinant Bacillus Subtilis

scholarly journals The Anti-Rotaviral Activity of Low Molecular Weight and Non-Proteinaceous Substance from Bifidobacterium longum BORI Cell Extract

2019 ◽  
Vol 7 (4) ◽  
pp. 108
Author(s):  
Yeo Ok Han ◽  
Yunju Jeong ◽  
Hyun Ju You ◽  
Seockmo Ku ◽  
Geun Eog Ji ◽  
...  
Keyword(s):  
Clinical Trial ◽  
Molecular Weight ◽  
Cytopathic Effect ◽  
Diarrheal Disease ◽  
Bifidobacterium Longum ◽  
Cell Extract ◽  
Host Cells ◽  
Low Molecular Weight ◽  
Protein Components ◽  
The Relationship

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.

scholarly journals Low-Molecular-Weight Pectate Lyase from Streptomyces thermocarboxydus

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

scholarly journals Low-Molecular-Weight Protein Tyrosine Phosphatases of Bacillus subtilis

2005 ◽  
Vol 187 (14) ◽  
pp. 4945-4956 ◽  
Author(s):  
Lucia Musumeci ◽  
Cristina Bongiorni ◽  
Lutz Tautz ◽  
Robert A. Edwards ◽  
Andrei Osterman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Stress Resistance ◽  
Ethanol Stress ◽  
Low Molecular Weight ◽  
Molecular Weight Protein ◽  
Gram Negative ◽  
Protein Tyrosine ◽  
Weight Protein ◽  
Low Molecular Weight Protein

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.

Characterization of a new efficient low molecular weight Bacillus subtilis NRC 16 levansucrase and its levan

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 ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Low Molecular Weight

scholarly journals Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis

1998 ◽  
Vol 180 (18) ◽  
pp. 4967-4973 ◽  
Author(s):  
Lotte B. Pedersen ◽  
Thomas Murray ◽  
David L. Popham ◽  
Peter Setlow
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Binding Protein ◽  
Low Molecular Weight ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Genome Sequencing Project ◽  
Penicillin Binding Proteins ◽  
Sequencing Project

ABSTRACT The pbp gene (renamed dacC), identified by the Bacillus subtilis genome sequencing project, encodes a putative 491-residue protein with sequence homology to low-molecular-weight penicillin-binding proteins. Use of a transcriptional dacC-lacZ fusion revealed thatdacC expression (i) is initiated at the end of stationary phase; (ii) depends strongly on transcription factor ςH; and (iii) appears to be initiated from a promoter located immediately upstream of yoxA, a gene of unknown function located upstream of dacC on the B. subtilis chromosome. A B. subtilis dacCinsertional mutant grew and sporulated identically to wild-type cells, and dacC and wild-type spores had the same heat resistance, cortex structure, and germination and outgrowth kinetics. Expression ofdacC in Escherichia coli showed that this gene encodes an ∼59-kDa membrane-associated penicillin-binding protein which is highly toxic when overexpressed.

scholarly journals Solution Structure of a Low-Molecular-Weight Protein Tyrosine Phosphatase from Bacillus subtilis

2006 ◽  
Vol 188 (4) ◽  
pp. 1509-1517 ◽  
Author(s):  
Huimin Xu ◽  
Bin Xia ◽  
Changwen Jin
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
Active Site ◽  
Solution Structure ◽  
Catalytic Mechanism ◽  
Backbone Dynamics ◽  
Low Molecular Weight ◽  
Hydrogen Bond Interaction ◽  
Protein Tyrosine ◽  
Loop Region

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.

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