M. I. Rajoka

686 total citations
29 papers, 572 citations indexed

About

M. I. Rajoka is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, M. I. Rajoka has authored 29 papers receiving a total of 572 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 16 papers in Biotechnology and 15 papers in Biomedical Engineering. Recurrent topics in M. I. Rajoka's work include Enzyme Production and Characterization (16 papers), Biofuel production and bioconversion (14 papers) and Enzyme Catalysis and Immobilization (12 papers). M. I. Rajoka is often cited by papers focused on Enzyme Production and Characterization (16 papers), Biofuel production and bioconversion (14 papers) and Enzyme Catalysis and Immobilization (12 papers). M. I. Rajoka collaborates with scholars based in Pakistan, Australia and United States. M. I. Rajoka's co-authors include Muhammad Hamid Rashid, Khawar Sohail Siddiqui, Ikram ul Haq, Amber Yasmeen, A.M. Khalid, Muhammad Siddique Awan, Abdul Jabbar, Muhammad Saleem, Raheela Perveen and Farooq Latif and has published in prestigious journals such as Bioresource Technology, Process Biochemistry and Biotechnology Progress.

In The Last Decade

M. I. Rajoka

29 papers receiving 524 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
M. I. Rajoka Pakistan	15	382	305	304	124	90	29	572
João Atílio Jorge Brazil	17	355 0.9×	279 0.9×	380 1.3×	256 2.1×	269 3.0×	41	746
Haroldo Yukio Kawaguti Brazil	12	174 0.5×	155 0.5×	242 0.8×	103 0.8×	83 0.9×	23	444
Jacques Georis Belgium	11	327 0.9×	390 1.3×	419 1.4×	83 0.7×	199 2.2×	14	629
Davender Kumar India	8	334 0.9×	280 0.9×	240 0.8×	45 0.4×	72 0.8×	10	497
César Rafael Fanchini Terrasan Brazil	17	492 1.3×	531 1.7×	384 1.3×	95 0.8×	187 2.1×	33	820
Swetha Sivaramakrishnan India	9	276 0.7×	192 0.6×	376 1.2×	147 1.2×	210 2.3×	12	602
Dhanya Gangadharan India	10	324 0.8×	213 0.7×	409 1.3×	170 1.4×	192 2.1×	16	666
Kakoli Dutt India	11	256 0.7×	148 0.5×	240 0.8×	66 0.5×	137 1.5×	22	482
Sreedharan Sajith India	13	284 0.7×	149 0.5×	167 0.5×	75 0.6×	79 0.9×	21	461
Nawel Boucherba Algeria	14	241 0.6×	230 0.8×	239 0.8×	68 0.5×	86 1.0×	27	440

Countries citing papers authored by M. I. Rajoka

Since Specialization

Citations

This map shows the geographic impact of M. I. Rajoka'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 M. I. Rajoka with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites M. I. Rajoka more than expected).

Fields of papers citing papers by M. I. Rajoka

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M. I. Rajoka. 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 M. I. Rajoka. The network helps show where M. I. Rajoka may publish in the future.

Co-authorship network of co-authors of M. I. Rajoka

This figure shows the co-authorship network connecting the top 25 collaborators of M. I. Rajoka. A scholar is included among the top collaborators of M. I. Rajoka 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 M. I. Rajoka. M. I. Rajoka is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Nadeem, Shahid, et al.. (2014). Optimizing different vitamins for L-glutamic acid production by Brevibacterium strain NIAB SS59.. Pakistan Journal of Zoology. 46(3). 733–739. 2 indexed citations

Nadeem, Shahid, et al.. (2011). Optimising Carbon and Nitrogen Sources for L-Glutamic acid Production by Brevibacterium strain NIAB SS-67. Pakistan Journal of Zoology. 43(2). 285–290. 3 indexed citations

Awan, Muhammad Siddique, et al.. (2010). Influence of nitrogen sources on production of β- galactosidase by Aspergillus niger. AFRICAN JOURNAL OF BIOTECHNOLOGY. 9(20). 2918–2922. 7 indexed citations

Awan, Muhammad Siddique, et al.. (2010). Gamma radiation induced mutagenesis in Aspergillus niger to enhance its microbial fermentation activity for industrial enzyme production. Molecular Biology Reports. 38(2). 1367–1374. 47 indexed citations

Naz, Sumera, et al.. (2010). Enhanced production and characterization of a β-glucosidase from Bacillus halodurans expressed in Escherichia coli. Biochemistry (Moscow). 75(4). 513–518. 14 indexed citations

Rajoka, M. I. & Amber Yasmeen. (2005). Improved productivity of β-fructofuranosidase by a derepressed mutant of Aspergillus niger from conventional and non-conventional substrates. World Journal of Microbiology and Biotechnology. 21(4). 471–478. 13 indexed citations

Rajoka, M. I. & Amber Yasmeen. (2005). Induction, and production studies of a novel glucoamylase of Aspergillus niger. World Journal of Microbiology and Biotechnology. 21(2). 179–187. 26 indexed citations

Rajoka, M. I., et al.. (2004). Kinetics of improved productivity of β-galactosidase by a cycloheximide-resistant mutant of Kluyveromyces marxianus. Biotechnology Letters. 26(9). 741–746. 17 indexed citations

Rajoka, M. I., et al.. (2004). Kinetics of enhanced ethanol productivity using raw starch hydrolyzing glucoamylase from Aspergillus niger mutant produced in solid state fermentation. Letters in Applied Microbiology. 39(1). 13–18. 10 indexed citations

10.

Rajoka, M. I., et al.. (2004). Kinetics of improved production and thermostability of an intracellular β-glucosidase from a mutant-derivative of Cellulomonas biazotea. Biotechnology Letters. 26(4). 281–285. 14 indexed citations

11.

Iqbal, Zafar, Muhammad Hamid Rashid, Abdul Jabbar, et al.. (2003). Kinetics of enhanced thermostability of an extracellular glucoamylase from Arachniotus sp.. Biotechnology Letters. 25(19). 1667–1670. 20 indexed citations

12.

Haq, Ikram ul, et al.. (2002). Production of lipases by Rhizopus oligosporous by solid-state fermentation. Process Biochemistry. 37(6). 637–641. 94 indexed citations

13.

Afzal, Ahmed J., et al.. (2002). Coupling of Surface Carboxyls of Carboxymethylcellulase with Aniline via Chemical Modification: Extreme Thermostabilization in Aqueous and Water‐Miscible Organic Mixtures. Biotechnology Progress. 18(2). 276–281. 7 indexed citations

14.

Parvez, Shoukat, et al.. (2002). Kinetics of β-glucosidase production by Escherichia coli recombinants harboring heterologous bgl genes. Biotechnology Letters. 24(21). 1803–1806. 3 indexed citations

15.

Parvez, Shoukat, et al.. (1998). Citric acid production from sugar cane molasses by 2-deoxyglucose-resistant mutant strain ofAspergillus niger. Folia Microbiologica. 43(1). 59–62. 17 indexed citations

16.

Rajoka, M. I., et al.. (1998). Cloning and expression of β-glucosidase genes inEscherichia coli andSaccharomyces cerevisiae using shuttle vector pYES 2.0. Folia Microbiologica. 43(2). 129–135. 18 indexed citations

17.

Siddiqui, Khawar Sohail, Muhammad Hamid Rashid, & M. I. Rajoka. (1997). Kinetic analysis of the active site of an intracellular β-glucosidase fromCellulomonas biazotea. Folia Microbiologica. 42(1). 53–8. 20 indexed citations

18.

Siddiqui, Khawar Sohail, et al.. (1997). Stability and identification of active-site residues of carboxymethylcellulases fromAspergillus niger andCellulomonas biazotea. Folia Microbiologica. 42(4). 312–318. 37 indexed citations

19.

Siddiqui, Khawar Sohail, et al.. (1997). Purification and the effect of manganese ions on the activity of carboxymethylcellulases fromAspergillus niger andCellulomonas biazotea. Folia Microbiologica. 42(4). 303–311. 16 indexed citations

20.

Siddiqui, Khawar Sohail, et al.. (1996). Activity and thermostability of carboxymethylcellulase from Aspergillus niger is strongly influenced by noncovalently attached polysaccharides. World Journal of Microbiology and Biotechnology. 12(3). 213–216. 28 indexed citations

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