Recent Advances in Enzyme Engineering through Incorporation of Unnatural Amino Acids

Won, Yumi; Pagar, Amol D.; Patil, Mahesh D.; Dawson, Philip E.; Yun, Hyungdon

doi:10.1007/s12257-019-0163-x

Cited by 23 publications

(28 citation statements)

References 99 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Manipulating the protein translation machinery for direct incorporation of ncAAs is another desirable approach, which enables the introduction of novel functionalities and reactivities beyond those offered by the 20 cAAs. Incorporating ncAAs into proteins has been widely applied in biocatalysis to enhance the activity and selectivity of enzymes, and even allows researchers to obtain novel catalytic reactions that are naturally unavailable [ [53] , [54] , [55] ]. This section presents some of the recent examples of using the genetic code expansion method to incorporate ncAAs into the POIs.…”

Section: Chemical Modifications Of Proteinsmentioning

confidence: 99%

Chemical modifications of proteins and their applications in metalloenzyme studies

Naowarojna

Cheng

Lopez

et al. 2021

Synthetic and Systems Biotechnology

View full text Add to dashboard Cite

Protein chemical modifications are important tools for elucidating chemical and biological functions of proteins. Several strategies have been developed to implement these modifications, including enzymatic tailoring reactions, unnatural amino acid incorporation using the expanded genetic codes, and recognition-driven transformations. These technologies have been applied in metalloenzyme studies, specifically in dissecting their mechanisms, improving their enzymatic activities, and creating artificial enzymes with non-natural activities. Herein, we summarize some of the recent efforts in these areas with an emphasis on a few metalloenzyme case studies.

show abstract

Section: Chemical Modifications Of Proteinsmentioning

confidence: 99%

Chemical modifications of proteins and their applications in metalloenzyme studies

Naowarojna

Cheng

Lopez

et al. 2021

Synthetic and Systems Biotechnology

View full text Add to dashboard Cite

show abstract

“…We can expect that more and more amino acids will be discovered and synthesized in the future. Incorporating unnatural amino acids into peptide and protein sequences is the object of intensive investigations [ 52 , 53 , 54 ].…”

Section: Annotation Of Amino Acids and Phosphate Groupsmentioning

confidence: 99%

Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using Biological and Chemical Codes

et al. 2021

View full text Add to dashboard Cite

Phosphorylation represents one of the most important modifications of amino acids, peptides, and proteins. By modifying the latter, it is useful in improving the functional properties of foods. Although all these substances are broadly annotated in internet databases, there is no unified code for their annotation. The present publication aims to describe a simple code for the annotation of phosphopeptide sequences. The proposed code describes the location of phosphate residues in amino acid side chains (including new rules of atom numbering in amino acids) and the diversity of phosphate residues (e.g., di- and triphosphate residues and phosphate amidation). This article also includes translating the proposed biological code into SMILES, being the most commonly used chemical code. Finally, it discusses possible errors associated with applying the proposed code and in the resulting SMILES representations of phosphopeptides. The proposed code can be extended to describe other modifications in the future.

show abstract

“…Biologically active enzymes are more costly than chemical catalysts, but they have the advantage of being environmentally friendly. They can lead to energy savings by reacting at lower temperature and pressure conditions while reducing residue formation [ 7 , 8 ]. Enzymatic-mediated production of flavor esters is an attractive process that allows to optimize several reaction factors such as concentration of reactants, reaction time, temperature, and activity of the immobilized enzyme [ 4 , 9 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

et al. 2020

View full text Add to dashboard Cite

Octyl formate is an important substance used in the perfume industry in products such as cosmetics, perfumes, and flavoring. Octyl formate is mostly produced by chemical catalysts. However, using enzymes as catalysts has gathered increasing interest due to their environment-friendly proprieties. In the present study, we aimed to identify the optimal conditions for the synthesis of octyl formate through immobilized enzyme-mediated esterification. We investigated the effects of enzymatic reaction parameters including the type of immobilized enzyme, enzyme concentration, molar ratio of reactants, reaction temperature, and type of solvent using the optimization method of one factor at a time (OFAT). The maximum conversion achieved was 96.51% with Novozym 435 (15 g/L), a 1:7 formic acid to octanol ratio, a reaction temperature of 40 °C, and with 1,2-dichloroethane as solvent. Moreover, we demonstrated that the Novozym 435 can be reused under the optimal conditions without affecting the octyl formate yield, which could help reduce the economic burden associated with enzymatic synthesis.

show abstract

Recent Advances in Enzyme Engineering through Incorporation of Unnatural Amino Acids

Cited by 23 publications

References 99 publications

Chemical modifications of proteins and their applications in metalloenzyme studies

Chemical modifications of proteins and their applications in metalloenzyme studies

Proposal of the Annotation of Phosphorylated Amino Acids and Peptides Using Biological and Chemical Codes

Enzymatic Synthesis of Formate Ester through Immobilized Lipase and Its Reuse

Contact Info

Product

Resources

About