Qualification:

• B. Sc.(1985)Zoology, Botany,Chemistry. Univ. of the Punjab, Lahore.(Government College, Lahore).
• M. Sc.(1988)Zoology (Cell & molecular Biology, Immunology, Genetics, Biochemistry etc.) Univ. of the Punjab, Lahore.(Government College, Lahore).
• Ph. D(1998)Zoology (Enzyme Engineering/ Biotechnology) Univ. of the Punjab, Lahore.
• Post Doc(2002-2004) Gene Cloning and Expression. Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Japan.

Awards/ Honors:

• Productive Scientist award from Ministry of Science and Technology, Pakistan for year-2002.
• Award of Post Doctoral fellowship on worldwide competition basis from “Japan Society for the Promotion of Science” (JSPS), Japan (May, 2002 to May, 2004).
• Invited guest speaker in “ASEAN Biochemistry Seminar/Workshop” at Surabaya Indonesia, 6-10 February, 2006.
• Award of “Enzyme Conferences International Fellowship” to present paper at “Symposium
• on Enzyme Engineering XIX, Sept., 23-28, 2007, British Columbia, Canada”
• Productive Scientist award from Ministry of Science and Technology, Pakistan for year-2008.
• Productive Scientist award from Ministry of Science and Technology, Pakistan for year-2010.
• Productive Scientist award from Ministry of Science and Technology, Pakistan for year-2011.
• Productive Scientist award from Ministry of Science and Technology, Pakistan for years-2012.
• Selection as external PhD examiner/ Jury member by Marseilles University, France. (PhD Exam conducted on 7^th June, 2013).

Research Interests

 1- Development of super Koji (Aspergillus oryzae), a hyper producer of food grade enzymes (α-amylases, cellulases, proteases, phytases, lipases, etc)

Pakistan’s almost complete enzymes demand is fulfilled through the imports and has spent 32.13 M US $ on the import of enzymes (Trade Map, 2018). According to Pakistan’s Economic Survey-2018, livestock shared 58.92% in agriculture. Recently, we have developed Koji (Aspergillus oryzae) mutant M100-6 strain, which is hyper producer of thermostable α-amylases and endoglucanase (Aleem et al., 2019). The Koji has GRAS (Generally Recognized as Safe) status, so safe for applications in food and feed industry. We are interested to further improve M100-6 Koji strain through genetic engineering to develop a super Koji having enhanced production of thermostable enzymes like: lipases, phytases, proteases, etc for applications in industries: food & feed, textile, paper & pulp, detergents, maltose syrup production, etc. Poultry industry is one of the most prepared & exciting sectors of Pakistan’s agriculture industry, which created source of employment to over 1.5 million people. The contribution of poultry meat (1.39 million tons) to the total meat production of Pakistan was 32.7% of the total meat.

Our goals are to develop super Koji strains having hyper production of thermostable enzymes and process up-scaling for the local production of food grade enzymes at industrial scale. Hence, the project will result into the development of technologies for the indigenous production of efficient food grade enzymes, which will save valuable foreign exchange. Moreover, the project has significance as it will help to generate employment by promoting various industries in the country. The use of livestock feed enzymes will be beneficial for environment and will reduce the production of gases in the sheds, which will protect the livestock farmers from ill hazards of the dangerous gases. Moreover, the local production of food grade enzymes will save foreign exchange worth of millions of US $.

2- Enzyme Immobilization:

Enzyme immobilization can improve enzymes operational stability, reactivity, specificity and structural rigidity. Nano-structured carriers are considered ideal material for enzyme immobilization because of having high surface area, outstanding dispersibility, and low mass transfer resistance but nanoporous materials are more demanding  because of being  more flexible for reactors and rigid enough to withstand high pressure and being quite fragile can be frayed and hardened by dehydration or an intense cross linking. That’s why most researchers chose porous nanomaterials support for immobilization of enzymes. Functionalized magnetic nanoparticles have been used for immobilization but are complicated to operate and easily lead to inactivation of the biocatalyst.

Metal Organic Frameworks (MOFs) are the most recently new reported porous polymeric platform for enzymatic catalysis. MOFs are the porous crystalline hybrid polymers consist of metal ions connected together by organic bridging ligand. By immobilization of enzyme in MOFs, the affinity of enzyme with substrate and catalytic activity can be increased. Taken together, MOFs and advanced porous materials are favoured choice for enzyme immobilization.

The α-amylase produce of super Koji will be immobilized on MOFs. Moreover, attempts will be made to develop better supports for efficient immobilization of enzymes for enhancing its catalytic activity, thermo stability, storage stability and reusability.

Publications in International Journals:

• Yasin, M.Z. and Rashid, M.H*. (2019). Purification and Extreme Thermostabilization of Glucoamylase by Zinc Produce of Novel Fungus Gymnoascella citrina. Process Biochemistry (In Press) (I.F.: 2.516; Citation: 0).
• Sher, H., Ali, H., Rashid, M.H*., Iftikhar, F., Saif-ur-Rehman, Nawaz, M.S., Khan, W.S. (2019)  Enzyme Immobilization on Metal-Organic Framework (MOF): Effects on Thermosability and Function. Proteins & Peptide Letters (In Press) (I.F.: 1.068; Citation: 0).
• Javed, M.R., Noman, M, Shahid, M, Ahmed, T, Khurshid, M, Rashid, M.H., Ismail, M., Sadaf, M. and Khan, F. (2019). Current situation of biofuel production and its enhancement by CRISPR/Cas9-mediated genome engineering of microbial cells. Microbiological Research, 219:1-11(I.F.= 2.777)
• Aleem, B., Rashid, M.H., Zeb, N., Saqib, A., Ihsan, A., Iqbal, M. and Ali, H. (2018). Random Mutagenesis of Super Koji (Aspergillus oryzae): Improvement in Production and Thermal Stability of α-Amylases for Maltose Syrup Production. BMC Microbiology 18:200. (I.F.= 2.829) https://doi.org/10.1186/s12866-018-1345-y.
• Gull, S., Rashid, M.H., Aftab, K., Umbreen, H., Kamal, S., Batool, S. and Noreen, R. (2018). Effect of metal Ions on kinetics and thermostability of α-amylase isolated from Aspergillus oryzae. Int. J. Agric. Biol., 20: 1267–1273. (I.F.= 0.902).
• Javed, M.R., Rashid, M.H., Riaz, M., Nadeem, H, Qasim, M. and Ashiq, N. (2018) Physiochemical and Thermodynamic Characterization of Highly Active Mutated Aspergillus niger β-glucosidase for Lignocellulose Hydrolysis. Protein & Peptide Letters 25(2): 208-219 DOI: 10.2174/0929866525666180130161504 (In Press: I.F.= 1.068)
• Javed, M.R., Buthe, A., Rashid, M.H. and Wang, P. (2016): Cost efficient entrapment of β-glucosidase in nanoscale latex and silicone polymeric thin films for use as stable biocatalysts. Food Chem. 190: 1078-1085 (I.F.: 3.391, Citation: 0).
• Nadeem, H., Rashid, M.H. and Siddique, M.H. (2015): Effect of Mg2+ and Al3+ ions on thermodynamic and physiochemical properties of Aspergillus niger invertases. Protein and Peptide Letters 22: 743-749 (I.F.: 1.068, Citation: 0)
• Nadeem, H., Rashid, M.H., et. al., (2015): Microbial Invertases: a Review on Kinetics, Thermodynamics and Physiochemical Characterization. Process Biochemistry 50: 1202- 1210 (I.F.: 2.516, Citation: 1).
• Huma, T., Rashid, M.H., Javed, M.R. and Ashraf, A. (2012). Gamma ray mediated mutagenesis of Phialocephala humicola: Effect on kinetics and thermodynamics of ?-amylase production. Afr. J. Microbiol. Res. 6: 4639-4646 (I.F.: 0.00; Citation: 0).
• Riaz, M., Rashid, M.H., Sawyer, L., Akhtar, S., Javed, M.R., Nadeem, H. and Wear, M. (2012). Physiochemical properties and kinetics of glucoamylase produced from deoxy-D-glucose resistant mutant of Aspergillus niger for soluble starch hydrolysis. Food Chem. 130: 24-30 (I.F.: 3.391; Citation: 8).
• Javed, M.R., Rashid, M.H., Mukhtar, Z., Riaz, M., Nadeem, H., Huma, T. and Ashiq, N. (2011). Kinetics and thermodynamics of high level β-glucosidase production by mutant derivative of Aspergillus niger under submerged growth conditions. Afr. J. Microbiol. Res. 5: 2528-2538. (I.F.: 0.00; Citation: 5).
• Niaz, M., Iftikhar, T., Rashid, M.H. (2011). Carboxyl group modification of Gymnoascella citrina glucoamylase: Cross-linking with hydrophobic nucleophile enhanced thermostability and thermophilicity. Clin. Biochem., 44(13): S93-S94. (I.F.: 2.275; Citation: 1).
• Nadeem, H., Rashid, M.H., Riaz, M., Asma, B., Javed, M.R. and Perveen, R. (2009). Invertase from Hyper Producer Strain of Aspergillus niger: Physiochemical Properties, Thermodynamics and Active Site Residues Heat of Ionization. Protein Pept. Lett.16:1098-1105. (I.F.: 1.068; Citation: 10).