scholarly journals A simple method for expression and purification of Shiga toxin 1 (Stx1) with biological activities by using a single-promoter vector and native signal peptide

2015 ◽  
Vol 63 (4) ◽  
pp. 539-545 ◽  
Author(s):  
Wei Tu ◽  
Tao Li ◽  
Qin Wang ◽  
Kun Cai ◽  
Xiang Gao ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Shiga Toxin ◽  
Biological Activities ◽  
Expression And Purification ◽  
Simple Method ◽  
Native Signal Peptide ◽  
Single Promoter

Extracellular expression of YlLip11 with a native signal peptide from Yarrowia lipolytica MSR80 in three different yeast hosts

2015 ◽  
Vol 110 ◽  
pp. 138-144 ◽  
Author(s):  
Arti Kumari ◽  
Keith Baronian ◽  
Gotthard Kunze ◽  
Rani Gupta
Keyword(s):  
Yarrowia Lipolytica ◽  
Signal Peptide ◽  
Extracellular Expression ◽  
Native Signal Peptide

scholarly journals Secretory expression of thermostable alkaline protease from Bacillus stearothermophilus FI by using native signal peptide and α-factor secretion signal in Pichia pastoris

2013 ◽  
Vol 88 (2) ◽  
pp. 85-91 ◽  
Author(s):  
Amaliawati Ahmad Latiffi ◽  
Abu Bakar Salleh ◽  
Raja Noor Zaliha Raja Abd. Rahman ◽  
Siti Nurbaya Oslan ◽  
Mahiran Basri
Keyword(s):  
Pichia Pastoris ◽  
Signal Peptide ◽  
Alkaline Protease ◽  
Bacillus Stearothermophilus ◽  
Secretory Expression ◽  
Secretion Signal ◽  
Factor Secretion ◽  
Native Signal Peptide

scholarly journals Engineering Signal Peptides for Enhanced Protein Secretion from Lactococcus lactis

2012 ◽  
Vol 79 (1) ◽  
pp. 347-356 ◽  
Author(s):  
Daphne T. W. Ng ◽  
Casim A. Sarkar
Keyword(s):  
Amino Acid ◽  
Lactococcus Lactis ◽  
Protein Secretion ◽  
Signal Peptide ◽  
Peptide Sequence ◽  
Signal Peptides ◽  
Biotechnological Production ◽  
Content Type ◽  
Amino Acid Mutagenesis ◽  
Native Signal Peptide

ABSTRACTLactococcus lactisis an attractive vehicle for biotechnological production of proteins and clinical delivery of therapeutics. In many such applications using this host, it is desirable to maximize secretion of recombinant proteins into the extracellular space, which is typically achieved by using the native signal peptide from a major secreted lactococcal protein, Usp45. In order to further increase protein secretion fromL. lactis, inherent limitations of the Usp45 signal peptide (Usp45sp) must be elucidated. Here, we performed extensive mutagenesis on Usp45sp to probe the effects of both the mRNA sequence (silent mutations) and the peptide sequence (amino acid substitutions) on secretion. We screened signal peptides based on their resulting secretion levels ofStaphylococcus aureusnuclease and further evaluated them for secretion ofBacillus subtilisα-amylase. Silent mutations alone gave an increase of up to 16% in the secretion of α-amylase through a mechanism consistent with relaxed mRNA folding around the ribosome binding site and enhanced translation. Targeted amino acid mutagenesis in Usp45sp, combined with additional silent mutations from the best clone in the initial screen, yielded an increase of up to 51% in maximum secretion of α-amylase while maintaining secretion at lower induction levels. The best sequence from our screen preserves the tripartite structure of the native signal peptide but increases the positive charge of the n-region. Our study presents the first example of an engineeredL. lactissignal peptide with a higher secretion yield than Usp45sp and, more generally, provides strategies for further enhancing protein secretion in bacterial hosts.

Improved production of holotoxin Stx2 with biological activities by using a single-promoter vector and an auto-induction expression system

2009 ◽  
Vol 67 (2) ◽  
pp. 169-174 ◽  
Author(s):  
Wei Tu ◽  
Kun Cai ◽  
Xiang Gao ◽  
Le Xiao ◽  
Rongchang Chen ◽  
...  
Keyword(s):  
Biological Activities ◽  
Expression System ◽  
Single Promoter

scholarly journals Construction of a novel secretion expression system guided by native signal peptide of PhoD inZymomonas mobilis

2014 ◽  
Vol 78 (4) ◽  
pp. 708-713 ◽  
Author(s):  
Bo Wu ◽  
Ming-Xiong He ◽  
Hong Feng ◽  
Zong-Xia Shui ◽  
Xiao-Yu Tang ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Expression System ◽  
Secretion Expression ◽  
Native Signal Peptide

scholarly journals Simple Method of 9,10-Anthraquinone Assay in Eleutherine americana (Aubl.) Merr. ex K. Heyne using High-Performance Liquid Chromatography

2021 ◽  
Vol 21 (6) ◽  
pp. 1389
Author(s):  
Sophi Damayanti ◽  
Samuel Gunadi Tanusondjaja ◽  
Benny Permana ◽  
Rika Hartati ◽  
Dian Ayu Eka Pitaloka ◽  
...  
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Mobile Phase ◽  
High Performance ◽  
Biological Activities ◽  
Simple Method ◽  
Accuracy Test ◽  
System Validation ◽  
System Suitability ◽  
Eleutherine Americana

Eleutherine americana (E. americana) is a medicinal plant commonly found on the island of Borneo, Indonesia. This plant is known to have several biological activities. However, anthraquinone residues are generally present as contaminants. This study was aimed to develop a method of determining the levels of 9,10-anthraquinone in plant extracts and fractions using High Performance Liquid Chromatography (HPLC). The research aims to optimize the mobile phase, the system suitability test, and the system validation. The optimal mobile phase was acetonitrile:distilled water 1:1 v/v with a flow rate of 1.25 mL/min. The validation result shows that the linearity was obtained with a correlation coefficient (r) of 0.9995 and an r2 coefficient of 0.9991. The estimated limits for detection and quantification values were 0.178 and 0.594 µg/mL, respectively. In the intraday and inter-day accuracy test, the coefficient of variance for reference was 0.627 and 0.774, while the results for the sample were 2.966 and 2.658. The percentage recovery rate for reference was between 98.976–101.452%, and for the sample, the result was 89.191–94.667%. The average 9,10-anthraquinone content in the acetate fraction of E. americana plant was 9.799 µg/g ± 5.243.

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