Santosh Kumar Padhi

1.1k total citations
37 papers, 868 citations indexed

About

Santosh Kumar Padhi is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Santosh Kumar Padhi has authored 37 papers receiving a total of 868 indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 8 papers in Spectroscopy and 7 papers in Materials Chemistry. Recurrent topics in Santosh Kumar Padhi's work include Enzyme Catalysis and Immobilization (27 papers), Microbial Metabolic Engineering and Bioproduction (16 papers) and Analytical Chemistry and Chromatography (7 papers). Santosh Kumar Padhi is often cited by papers focused on Enzyme Catalysis and Immobilization (27 papers), Microbial Metabolic Engineering and Bioproduction (16 papers) and Analytical Chemistry and Chromatography (7 papers). Santosh Kumar Padhi collaborates with scholars based in India, United States and Germany. Santosh Kumar Padhi's co-authors include Anju Chadha, Uwe T. Bornscheuer, Jon D. Stewart, Despina J. Bougioukou, Helge Jochens, Romas J. Kazlauskas, Ganesh N. Pandian, Robert Kourist, Konstanze Stiba and Martin Hesseler and has published in prestigious journals such as Journal of the American Chemical Society, Chemical Communications and ACS Catalysis.

In The Last Decade

Santosh Kumar Padhi

34 papers receiving 853 citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Santosh Kumar Padhi 741 174 131 130 120 37 868
Anders O. Magnusson 739 1.0× 179 1.0× 81 0.6× 161 1.2× 134 1.1× 14 883
Wolfgang Skranc 702 0.9× 362 2.1× 77 0.6× 91 0.7× 147 1.2× 29 986
Yoshihiko Yasohara 892 1.2× 213 1.2× 123 0.9× 78 0.6× 161 1.3× 34 1.0k
Sebastian Bartsch 928 1.3× 252 1.4× 164 1.3× 56 0.4× 110 0.9× 26 1.0k
Norbert Klempier 659 0.9× 317 1.8× 82 0.6× 92 0.7× 61 0.5× 41 833
Cecilia Branneby 650 0.9× 280 1.6× 85 0.6× 100 0.8× 84 0.7× 11 734
Pankaj Soni 638 0.9× 83 0.5× 79 0.6× 72 0.6× 158 1.3× 30 755
Denis Wahler 791 1.1× 175 1.0× 55 0.4× 306 2.4× 112 0.9× 24 956
Theo Sonke 937 1.3× 240 1.4× 104 0.8× 62 0.5× 140 1.2× 37 1.1k
Spiros Kambourakis 409 0.6× 299 1.7× 112 0.9× 44 0.3× 96 0.8× 21 679

Countries citing papers authored by Santosh Kumar Padhi

Since Specialization
Citations

This map shows the geographic impact of Santosh Kumar Padhi's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Santosh Kumar Padhi with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Santosh Kumar Padhi more than expected).

Fields of papers citing papers by Santosh Kumar Padhi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Santosh Kumar Padhi. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Santosh Kumar Padhi. The network helps show where Santosh Kumar Padhi may publish in the future.

Co-authorship network of co-authors of Santosh Kumar Padhi

This figure shows the co-authorship network connecting the top 25 collaborators of Santosh Kumar Padhi. A scholar is included among the top collaborators of Santosh Kumar Padhi based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Santosh Kumar Padhi. Santosh Kumar Padhi is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
2.
Israr, Muhammad, Santosh Kumar Padhi, Yi Zhou, & Shuke Wu. (2025). Recent Advances in Protein Engineering and Synthetic Applications of Amino Acid Transaminases. ChemCatChem. 17(8). 1 indexed citations
3.
Biswal, Bijesh Kumar, et al.. (2025). Gymnema saponin-induced lipid flip-flop identifies rigid membrane phenotype of methicillin resistant S. aureus and enhances it's antibiotic susceptibility. Archives of Biochemistry and Biophysics. 765. 110303–110303.
4.
Mohit, MOHIT, et al.. (2022). Biochemical characterization, substrate and stereoselectivity of an outer surface putative α/β hydrolase from the pathogenic Leptospira. International Journal of Biological Macromolecules. 229. 803–813.
5.
Padhi, Santosh Kumar, et al.. (2022). On the design of p-channel step-FinFET at sub-10nm node: A parametric analysis. Microelectronics Journal. 126. 105505–105505. 7 indexed citations
6.
Padhi, Santosh Kumar, et al.. (2021). One‐Pot Enzyme Cascade Catalyzed Asymmetrization of Primary Alcohols: Synthesis of Enantiocomplementary Chiral β‐Nitroalcohols. Advanced Synthesis & Catalysis. 363(23). 5310–5318. 14 indexed citations
7.
Padhi, Santosh Kumar, et al.. (2020). Immobilized Arabidopsis thaliana Hydroxynitrile Lyase-Catalyzed Retro-Henry Reaction in the Synthesis of (S)-β-Nitroalcohols. Applied Biochemistry and Biotechnology. 193(2). 560–576. 12 indexed citations
8.
Beier, Andy, David Kovář, Santosh Kumar Padhi, et al.. (2019). An Ultrasensitive Fluorescence Assay for the Detection of Halides and Enzymatic Dehalogenation. ChemCatChem. 12(7). 2032–2039. 12 indexed citations
9.
Padhi, Santosh Kumar, et al.. (2018). Immobilized Baliospermum montanum hydroxynitrile lyase catalyzed synthesis of chiral cyanohydrins. Bioorganic Chemistry. 84. 32–40. 14 indexed citations
10.
Padhi, Santosh Kumar, et al.. (2018). Production of (S)‐β‐Nitro Alcohols by Enantioselective C−C Bond Cleavage with an R‐Selective Hydroxynitrile Lyase. ChemBioChem. 20(3). 371–378. 15 indexed citations
11.
Chadha, Anju, et al.. (2016). Candida parapsilosis: A versatile biocatalyst for organic oxidation-reduction reactions. Bioorganic Chemistry. 68. 187–213. 25 indexed citations
12.
13.
Jochens, Helge, Martin Hesseler, Konstanze Stiba, et al.. (2011). Protein Engineering of α/β‐Hydrolase Fold Enzymes. ChemBioChem. 12(10). 1508–1517. 91 indexed citations
14.
Padhi, Santosh Kumar, et al.. (2010). Switching from an Esterase to a Hydroxynitrile Lyase Mechanism Requires Only Two Amino Acid Substitutions. Chemistry & Biology. 17(8). 863–871. 45 indexed citations
15.
Kourist, Robert, Helge Jochens, Sebastian Bartsch, et al.. (2010). The α/β‐Hydrolase Fold 3DM Database (ABHDB) as a Tool for Protein Engineering. ChemBioChem. 11(12). 1635–1643. 121 indexed citations
16.
Padhi, Santosh Kumar, Iwona Kaluzna, Didier Buisson, Robert Azerad, & Jon D. Stewart. (2007). Reductions of cyclic β-keto esters by individual Saccharomyces cerevisiae dehydrogenases and a chemo-enzymatic route to (1R,2S)-2-methyl-1-cyclohexanol. Tetrahedron Asymmetry. 18(18). 2133–2138. 17 indexed citations
17.
Padhi, Santosh Kumar, Titu Devamani, Ganesh N. Pandian, & Anju Chadha. (2006). Deracemisation of β-hydroxy esters using immobilised whole cells of Candida parapsilosis ATCC 7330: substrate specificity and mechanistic investigation. Tetrahedron. 62(21). 5133–5140. 44 indexed citations
18.
Padhi, Santosh Kumar & Anju Chadha. (2005). Deracemisation of aromatic β-hydroxy esters using immobilised whole cells of Candida parapsilosis ATCC 7330 and determination of absolute configuration by 1H NMR. Tetrahedron Asymmetry. 16(16). 2790–2798. 36 indexed citations
19.
Padhi, Santosh Kumar, Ganesh N. Pandian, & Anju Chadha. (2004). Microbial deracemisation of aromatic β-hydroxy acid esters. Journal of Molecular Catalysis B Enzymatic. 29(1-6). 25–29. 40 indexed citations
20.
Chadha, Anju & Santosh Kumar Padhi. (2003). Sodium Borohydride Reductionand Selective Transesterification of β-Keto Esters in aOne-pot Reaction under Mild Conditions. Synlett. 639–642. 8 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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