Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Microorganisms ; 9(6)2021 May 28.
Article in English | MEDLINE | ID: mdl-34071282

ABSTRACT

The microbial diversity in anaerobic digestion (AD) is important because it affects process robustness. High-throughput sequencing offers high-resolution data regarding the microbial diversity and robustness of biological systems including AD; however, to understand the dynamics of microbial processes, knowing the microbial diversity is not adequate alone. Advanced meta-omic techniques have been established to determine the activity and interactions among organisms in biological processes like AD. Results of these methods can be used to identify biomarkers for AD states. This can aid a better understanding of system dynamics and be applied to producing comprehensive models for AD. The paper provides valuable knowledge regarding the possibility of integration of molecular methods in AD. Although meta-genomic methods are not suitable for on-line use due to long operating time and high costs, they provide extensive insight into the microbial phylogeny in AD. Meta-proteomics can also be explored in the demonstration projects for failure prediction. However, for these methods to be fully realised in AD, a biomarker database needs to be developed.

2.
Comput Biol Chem ; 77: 272-278, 2018 Dec.
Article in English | MEDLINE | ID: mdl-30396154

ABSTRACT

Organophosphate compounds bioremediation by use of organophosphorus degradation enzymes such as DFPase is a developing interest in industry and medicine. The most important problem with the bio-catalytic enzymes is their instability on high temperatures. This work carried out to find suitable locations for introducing disulfide bridges in DFPase enzyme. We employed some computational approaches to design the disulfide bridges and evaluate their roles in the enzyme structural thermostability. According to the in silico results, mutant 6 (V24C, C76) increased the enzyme thermostability relative to wild-type.


Subject(s)
Loligo/enzymology , Phosphoric Triester Hydrolases/chemistry , Animals , Catalytic Domain , Databases, Protein , Disulfides/chemistry , Enzyme Stability , Hot Temperature , Loligo/chemistry , Loligo/genetics , Molecular Dynamics Simulation , Phosphoric Triester Hydrolases/genetics , Point Mutation , Protein Conformation
SELECTION OF CITATIONS
SEARCH DETAIL
...