Satya Prakash Singh
@saurashtrauniversity.edu
UGC-BSR Faculty Fellow (Professor-Emeritus)
Saurashtra University
Currently UGC-BSR Professor with Biosciences, Saurashtra University, Rajkot, India. Earlier, Professor & Head (2003-2020) in the same Department. Masters’ from G. B. Pant University of Agriculture & Technology, India, and Ph.D. from Griffith University, Australia. Visiting Scientist at National Food Research Institute, Tsukuba, Japan, and Visiting Professor at Yangon University, Myanmar. Published 110 research papers, 30 book chapters, and 1 edited book (Springer), with H-Index 34 and citations of around 3500. Supervised 25 Ph.D., 23 MPhil, and 110 MSc students; 3 Ph.D. and 4 Masters students currently working. Research collaborations with NFRI-Japan, Griffith University-Australia, IIT-Delhi, University of Delhi, Central University-Hyderabad, and JNTU-Hyderabad. Research Projects funded by UGC, DBT, CSIR, MoES, DST, GSBTM, Saurashtra University, and the Government of Japan.
EDUCATION
• PhD: Griffith University, Brisbane, Australia 1986
• M.Phil. (Partial): JNU-New Delhi 1981-82
• MSc: G. B. Pant University of Agriculture & Technology, Pantnagar 1980
• BSc: Avadh University, Ayodhya-Faizabad 1977
RESEARCH INTERESTS
Diversity, Phylogeny & Biocatalytic potential of halophilic/haloalkaliphilic bacteria; Hyperthermophilic bacteria /Protein Engineering: Structure & Function relationship; Metabolic regulation in Gram positive bacteria-In Vivo High Field NMR
Scopus Publications
Scholar Citations
Scholar h-index
Scholar i10-index
Scopus Publications
Bhavtosh Kikani, Rajesh Patel, Jignasha Thumar, Hitarth Bhatt, Dalip Singh Rathore, Gopi A. Koladiya, and Satya P. Singh
Elsevier BV
Nirali M. Raiyani and Satya P. Singh
Springer Science and Business Media LLC
Rushit J. Shukla and Satya P. Singh
Wiley
Sangeeta D. Gohel, Vaishali R. Majithiya, and Satya P. Singh
Informa UK Limited
Abstract Saline and alkaline habitats of the Okha coastline, Gujarat, India, were explored for the diversity of actinobacteria. Based on the phenotypic and genotypic heterogeneity, nine haloalkaliphilic actinobacterial strains were characterized and identified. The PCR amplification of 16S rDNA using universal and genus-specific primers corroborated the trends that emerged through cultural and physiological characterization. Streptomyces was the most abundant genus amplified with the Streptomyces-specific primers (StreptB/E, StreptB/F), whereas other actinobacterial strains were amplified by the universal primers U1 and U2. Further molecular diversity was investigated by the gradient PCR-DGGE as a fingerprinting tool that generated group-specific DGGE patterns. Based on the nucleotide homology and phylogenetic analysis, strains OK-1 and OK-2 were identified as Streptomyces somaliensis. At the same time, OK-3 and OK-7 were detected as Streptomyces sp., while OK-5, OK-6, OK-8, OK-9, and OK-10 belonged to Nocardiopsis alba. Further, the cluster analysis using the UPGMA method generated 3 clusters based on biochemical characterization, sugar utilization, and enzyme production. The dendrogram based on the DGGE band pattern created with Jaccard-distance revealed two major clades with 33.33% similarity. Further, the study of alpha diversity calculation using phenotypic characteristics discloses highly diverse sugar utilization abilities. Moreover, a stress value of 0.1236 was obtained based on the NMDS analysis of the plots using Bary-Curties dissimilarity. Overall, the distinct phenotypic, metabolic, and molecular profiling illustrated the diversity among marine actinobacteria.
Foram J. Thakrar, Gopi A. Koladiya, and Satya P. Singh
Springer Science and Business Media LLC
Ankita Dobariya, Gira P. Mankad, Hasti Ramavat, and Satya P. Singh
Springer Science and Business Media LLC
Megha K. Purohit, Dalip Singh Rathore, Gopi Koladiya, Sandeep Pandey, and Satya P. Singh
Springer Science and Business Media LLC
V. H. Raval, D. S. Rathore, and S. P. Singh
Pleiades Publishing Ltd
V. Raval, Rupal H. Joshi, Hitarth B. Bhatt and Satya P. Singh
Hitarth B. Bhatt and Satya P. Singh
Frontiers Media SA
Deserts in general, and Indian deserts in particular, are less attended for microbial diversity. The Little Rann of Kutch (LRK), a coastal saline desert, is characterized by a unique combination of both dry and wet features. This study represents the first report on the extensive isolation, spatial distribution, 16S rRNA gene-based phylogeny, and identification of novel taxa. A total of 87 isolates were obtained from three different study sites in LRK. Based on the full 16S rRNA gene sequences, the isolates were grouped into 44 different phylotypes of four phyla: Firmicutes, Proteobacteria, Actinobacteria, and Euryarchaeota. These in turn were represented by 19 different genera. Halomonas, Gracilibacillus, Thalassobacillus, Piscibacillus, Salimicrobium, Alkalibacillus, Bhargavaea, Proteus, Marinobacter, Pseudomonas, Kocuria, Corynebacterium, Planococcus, Micrococcus and Natronococcus identified in this study had never before been reported from this habitat. A majority of the isolates displayed broad salt and pH tolerance. The bacterial diversity of Venasar and Jogad closely resembled with each other. While Bacillus, Virgibacillus, Gracillibacillus, and Bhargavaea were common genera in all sites, six putative novel taxa of different phylogenetic groups were identified. Available nitrogen, pH, Organic carbon, TDS, and EC were the main environmental variables affecting the microbial diversity. Analysis of the geographical distribution revealed that a majority of the phylotypes had cosmopolitan distribution, followed by the saline and marine distribution, while ∼13% were affiliated with only LRK. The phylotypes associated with marine distribution decreased with increasing distance from the Gulf of Kutch, suggesting their endemism to marine environments. The study established the taxonomic novelty and prospects for the discovery of unique products and metabolites.
Jignasha Thumar and Satya P. Singh
Springer Nature Singapore
Hitarth B. Bhatt, Dhritiksha M. Baria, Vikram H. Raval, and Satya P. Singh
Elsevier
Kalpna D. Rakholiya, Mital J. Kaneria, Paragi R. Jadhav, and Satya P. Singh
Elsevier
Dalip Singh Rathore, Amit Kumar Sharma, Ankita Dobariya, Hashti Ramavat, and Satya P. Singh
Springer Nature Singapore
Nagendra Thakur, Satya P. Singh, and Changyi Zhang
Elsevier BV
Bhavtosh A. Kikani and Satya P. Singh
Informa UK Limited
Abstract Amylases hydrolyze starch to diverse products including dextrins and progressively smaller polymers of glucose units. Thermally stable amylases account for nearly 25% of the enzyme market. This review highlights the structural attributes of the α-amylases from thermophilic bacteria. Heterologous expression of amylases in suitable hosts is discussed in detail. Further, specific value maximization approaches, such as protein engineering and immobilization of the amylases are discussed in order to improve its suitability for varied applications on a commercial scale. The review also takes into account of the immobilization of the amylases on nanomaterials to increase the stability and reusability of the enzymes. The function-based metagenomics would provide opportunities for searching amylases with novel characteristics. The review is expected to explore novel amylases for future potential applications.
Purna Dwivedi, Amit K. Sharma, and Satya P. Singh
Elsevier BV
Dalip Singh Rathore and Satya P. Singh
Springer Science and Business Media LLC
Dalip Singh Rathore, Mahejbin A. Sheikh, Sangeeta D. Gohel, and Satya P. Singh
Springer Science and Business Media LLC
Jagruti V. Chauhan, Riddhi P. Mathukiya, Satya P. Singh, and Sangeeta D. Gohel
Elsevier BV
Amit K. Sharma, Bhavtosh A. Kikani, and Satya P. Singh
Informa UK Limited
Abstract The diversity and biotechnological potential of the haloalkaliphilic actinomycetes of the saline habitats are explored only in a limited sense. Albeit, they have been reported to produce various enzymes, organic acids, antibiotics, and other secondary metabolites. Therefore, we aimed to investigate marine actinomycetes with respect to their cultivation, morphology, biochemical properties, enzyme secretion, solvent tolerance, antibacterial activities and phylogeny. Further, the composition of cell wall and its sugar constituents and variation in multiple–antibiotic-resistance (MAR) suggested diversity of the actinomycetes of the studied habitats. In total, 20 haloalkaliphilic actinomycetes were identified and studied further. Based on the 16S rRNA gene sequences, most of these actinomycetes belong to the genus Nocardiopsis. However, Hae III restriction patterns of the 16S rRNA genes reveal eight main clusters, corresponding with the Jaccard’s similarity coefficient and phenograms based on the biochemical properties. The Canonical Correlation Analysis suggests that pH and temperature rather than salinity and conductivity of the saline habitat are determinants of the growth of actinomycetes. The polyphasic analysis was highly significant in judging the diversity and taxonomy of the marine actinomycetes. Besides, the evaluated phenetic attributes may help in the exploration of the biotechnological potential of these actinomycetes.
Nirali M. Raiyani and Satya P. Singh
Elsevier BV
Amit K. Sharma, Bhavtosh A. Kikani, and Satya P. Singh
Elsevier BV
Hitarth B. Bhatt and Satya P. Singh
Frontiers Media SA
An alkaline protease gene of Bacillus lehensis JO-26 from saline desert, Little Rann of Kutch, was cloned and expressed in Escherichia coli BL21 (DE3). A 1,014-bp ORF encoded 337 amino acids. The recombinant protease (APrBL) with Asp 97, His 127, and Ser 280 forming catalytic triad belongs to the subtilase S8 protease family. The gene was optimally expressed in soluble fraction with 0.2 mM isopropyl β-D-thiogalactopyranoside (IPTG), 2% (w/v) NaCl at 28°C. APrBL, a monomer with a molecular mass of 34.6 kDa was active over pH 8–11 and 30°C−70°C, optimally at pH 10 and 50°C. The enzyme was highly thermostable and retained 73% of the residual activity at 80°C up to 3 h. It was significantly stimulated by sodium dodecyl sulfate (SDS), Ca2+, chloroform, toluene, n-butanol, and benzene while completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and Hg2+. The serine nature of the protease was confirmed by its strong inhibition by PMSF. The APrBL gene was phylogenetically close to alkaline elastase YaB (P20724) and was distinct from the well-known commercial proteases subtilisin Carlsberg (CAB56500) and subtilisin BPN′ (P00782). The structural elucidation revealed 31.75% α-helices, 22.55% β-strands, and 45.70% coils. Although high glycine and fewer proline residues are a characteristic feature of the cold-adapted enzymes, the similar observation in thermally active APrBL suggests that this feature cannot be solely responsible for thermo/cold adaptation. The APrBL protease was highly effective as a detergent additive and in whey protein hydrolysis.
RECENT SCHOLAR PUBLICATIONS
MOST CITED SCHOLAR PUBLICATIONS
GRANT DETAILS
Research grants from MoES, Govt. of India; DBT as the Multi-Institutional Project with Saurashtra University; IIT Delhi and University of Delhi; UGC Projects/Programs: CAS, DSA and COSIST Programs and other projects; UGC-BSR Faculty Program; DST Infrastructural Project under FIST Program; GSBTM (Gujarat State Biotechnology Mission), Japan Research and Development Corporation: At NFRI, Tukuba, Japan; ICAR Sponsored Projects: at G. B. Pant University, Pantnagar, India
RESEARCH OUTPUTS (PATENTS, SOFTWARE, PUBLICATIONS, PRODUCTS)
1. PATENT APPLICATION PUBLICATION
Application , INDIA
Date of filing of Application:23/04/2021
Publication Date: 28/10/2022
2. PATENT APPLICATION PUBLICATION
Application A, INDIA (22)
Date of filing of Application:23/04/2021
Publication Date: 28/10/2022
3. PATENT APPLICATION PUBLICATION
Application A, INDIA (22)
Date of filing of Application:23/04/2021
Publication Date: 28/10/2022
Industry, Institute, or Organisation Collaboration
Research collaborations with Dr. Kiyoshi Hayashi (National Food Research Institute and now at Toyo University, Japan), Prof. Peter Rogers (Griffith University, Brisbane, Australia), Prof. S. K. Khare (IIT, New Delhi), and Prof. Sanjay Kapoor (University of Delhi University, South Campus, New Delhi), Central University of Hyderabad (Prof. Ch. Ramana Rao) and Jawaharlal Nehru Technological University, Hyderabad (Prof. Ch. Sasikala).