Haneef Rehman - Academia.edu (original) (raw)

Papers by Haneef Rehman

Research paper thumbnail of Production Of 3-Hydroxypropanoic Acid Using Hydrogel Compartmentalized Microbial Strains

2nd International Conference on Biological Research and Applied Science

Research paper thumbnail of Production Of 3-Hydroxypropanoic Acid Using Hydrogel Compartmentalized Microbial Strains

2nd International Conference on Biological Research and Applied Science, Jan 22, 2022

Research paper thumbnail of Applications of Pectinolytic Enzymes in Process Industries

IntechOpen eBooks, May 17, 2023

Research paper thumbnail of Development of Pectinase Based Nanocatalyst by Immobilization of Pectinase on Magnetic Iron Oxide Nanoparticles Using Glutaraldehyde as Crosslinking Agent

Molecules

To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobili... more To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobilized on iron oxide nanocarrier. Through co-precipitation, magnetic iron oxide nanoparticles were synthesized. Scanning electron microscopy (SEM) and energy dispersive electron microscopy (EDEX) were used to analyze the nanoparticles. Pectinase was immobilized using glutaraldehyde as a crosslinking agent on iron oxide nanocarrier. In comparison to free pectinase, immobilized pectinase demonstrated higher enzymatic activity at a variety of temperatures and pH levels. Immobilization also boosted pectinase’s catalytic stability. After 120 h of pre-incubation at 50 °C, immobilized pectinase maintained more than 90% of its initial activity due to the iron oxide nanocarrier, which improved the thermal stability of pectinase at various temperatures. Following 15 repetitions of enzymatic reactions, immobilized pectinase still exhibited 90% of its initial activity. According to the results, pectina...

Research paper thumbnail of Compartmentalization of Pectinase within Cellulose Hydrogel: An Efficient Technique to Enhance the Catalytic Properties of Pectinase for Industrial Applications

Austin Journal of Biotechnology & Bioengineering, 2021

Pectinase catalyze the breakdown of pectin polymer and widely has been used in different industri... more Pectinase catalyze the breakdown of pectin polymer and widely has been used in different industrial preparations such as fruit juice preparation, liquification and scarification of plant biomass as well as coffee and tea fermentation. In this study, the pectinase from Bacillus licheniformis was compartmentalized within cellulose beads hydrogel using encapsulation technique to make it reusable with easy recovery from reaction mixture. The compartmentalization improved catalytic properties of pectinase and ensured its reusability for continuous uses. It was observed that 5.0% cellulose concentration was enough to form stable cellulose hydrogel beads with retention of high relative of activity of pectinase. The hydrogel compartmentalization didn’t change the optima pH and temperature for maximum relative activity and both the hydrogel compartmentalized pectinase and free pectinase maximum relative at same pH and temperature but the hydrogel compartmentalization increased the stability ...

Research paper thumbnail of Degradation of complex carbohydrate: Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support

Research paper thumbnail of Encapsulation of pectinase within polyacrylamide gel: characterization of its catalytic properties for continuous industrial uses

Heliyon, 2020

Pectinase as a biocatalyst play a significant role in food and textile industries. In this study,... more Pectinase as a biocatalyst play a significant role in food and textile industries. In this study, the pectinase was immobilized by encapsulation within polyacrylamide gel to enhance its catalytic properties and ensure the reusability for continuous industrial processes. 9.5% acrylamide and 0.5% N, N′- methylenebisacrylamide concentration gave high percentage of pectinase immobilization yield within gel. The catalytic properties of immobilized pectinase was determined with comparison of soluble pectinase. The immobilization of pectinase within polyacrylamide gel didn't effect catalytic properties of pectinase and both the free and immobilized pectinase showed maximum pectinolytic activity at 45 °C and pH 10. The Michaelis-Menten kinetic behavior of pectinase was slightly changed after immobilization and immobilized pectinase showed somewhat higher Km and lower Vmax value as compared to soluble pectinase. Polyacrylamide gel encapsulation enhanced the thermal stability of pectinase...

Research paper thumbnail of Immobilization And Characterization Of Pectinase From Bacillus Species Using Different Supports

Research paper thumbnail of Role of Artemisia macrocephala as enzymes inhibitor in dementia and nociception! A pharmacological study

Pure and Applied Biology, 2016

Research paper thumbnail of Phytochemical analysis and antibacterial properties of Calotropis procera against bacterial phytopathogens

World Journal of Biology and Biotechnology

Calotropis procera, is known as crown flower or giant milkweed and belongs to the family Asclepia... more Calotropis procera, is known as crown flower or giant milkweed and belongs to the family Asclepiadacea. It has been traditionally used for various medicinal purposes. In the present study, the phytochemical analysis, antioxidant property, and antimicrobial activity of C. procera were evaluated. Methanol was used as a solvent for the extract preparation using soxhlet extraction. The extracts were subjected to the analysis of the different secondary bioactive metabolites. Furthermore, the antimicrobial activities of these extracts were determined against various pathogens. The qualitative analysis of plant extracts of leaves stems, and roots showed the presence of phenolic compounds, alkaloids, carbohydrates, glycosidic, protein, phytosterols, steroid, saponin, and flavonoid compounds. The leaf extract of C. procera plants inhibited 95% 2,2-diphenyl-1-picrylhydrazyl (DDPH) activity at 0.8 mg/mL Methanol extract of C. procera showed the maximum antibacterial and antifungal activities a...

Research paper thumbnail of Single step immobilization of CMCase within agarose gel matrix: Kinetics and thermodynamic studies

Colloids and Surfaces B: Biointerfaces

Research paper thumbnail of Utilization of different polymers for the improvement of catalytic properties and recycling efficiency of bacterial maltase

International Journal of Biological Macromolecules

Research paper thumbnail of Production of commercially important enzymes from Bacillus licheniformis KIBGE-IB3 using date fruit wastes as substrate

Journal of Genetic Engineering and Biotechnology

Research paper thumbnail of Xylan Deterioration Approach: Purification and catalytic behavior optimization of a novel β-1,4-D-xylanohydrolase from Geobacillus stearothermophilus KIBGE-IB29

Research paper thumbnail of Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Environmental Science and Pollution Research, 2016

In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable subs... more In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml(-1) of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel. It was evident from the results that bacterial isolate secreted 6539.0 U ml(-1) of α-1,4-glucosidase in the presence of 0.4% peptone and meat extract with 0.1% yeast extract. B. licheniformis KIBGE-IB4 released 6739.0 and 7190.0 U ml(-1) of enzyme at 40 °C and pH 7.0, respectively. An improved and cost-effective growth medium design resulted 8590.0 U ml(-1) of α-1,4-glucosidase with 1.3-fold increase as compared to initial amount from B. licheniformis KIBGE-IB4. This enzyme can be used to fulfill the accelerating demand of food and pharmaceutical industries. Further purification and immobilization of this enzyme can also enhance its utility for various commercial applications. Graphical abstract Pictorial representation of maltase production from sweet potato peel.

Research paper thumbnail of Maltase entrapment approach as an efficient alternative to increase the stability and recycling efficiency of free enzyme within agarose matrix

Journal of the Taiwan Institute of Chemical Engineers, 2016

Research paper thumbnail of Polyacrylamide Gel-Entrapped Maltase: An Excellent Design of Using Maltase in Continuous Industrial Processes

Applied Biochemistry and Biotechnology, 2016

Bacterial maltase catalyzes the hydrolysis of maltose and is known as one of the most significant... more Bacterial maltase catalyzes the hydrolysis of maltose and is known as one of the most significant hydrolases. It has several applications in different industrial processes but widely used in food fermentation technology and alcohol production. In the current study, entrapment technique was comprehensively examined using polyacrylamide gel as a matrix support to improve the stability and catalytic efficiency of maltase for continuous use. Maximum entrapment yield of maltase was achieved at 10 % polyacrylamide concentration with 3.0-mm bead size. Optimized conditions indicated an increase in the reaction temperature from 45 to 55 °C after maltase entrapment while no change was observed in the reaction time and pH. An increase in the K m value of entrapped maltase was attained whereas V max value decreased from 8411.0 to 6813.0 U ml(-1) min(-1) with reference to its free counterpart. Entrapped maltase showed remarkable thermal stability and retained 16 % activity at 70 °C even after 120.0 min. Entrapped maltase also exhibited excellent recycling efficiency up to eight consecutive reaction cycles. With respect to economic feasibility, entrapped maltase indicates its high potential to be used in various biotechnological applications.

Research paper thumbnail of The Biology of Balochistani Weed: Cyperus rotundus Linnaeus. A Review

Pure and Applied Biology, 2015

Research paper thumbnail of Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Biochemistry and Biophysics Reports, 2015

Research paper thumbnail of Immobilization of Pectin Depolymerising Polygalacturonase Using Different Polymers

International journal of biological macromolecules, Jan 7, 2015

Polygalacturonase catalyses the hydrolysis of pectin substances and widely has been used in food ... more Polygalacturonase catalyses the hydrolysis of pectin substances and widely has been used in food and textile industries. In current study, different polymers such as calcium alginate beads, polyacrylamide gel and agar-agar matrix were screened for the immobilization of polygalacturonase through entrapment technique. Polyacrylamide gel was found to be most promising one and gave maximum (89%) immobilization yield as compared to agar-agar (80%) and calcium alginate beads (46%). The polymers increased the reaction time of polygalacturonase and polymers entrapped polygalacturonases showed maximum pectinolytic activity after 10minutes of reaction as compared to free polygalacturonase which performed maximum activity after 5.0minutes of reaction time. The temperature of polygalacturonase for maximum enzymatic activity was increased from 45°C to 50°C and 55°C when it was immobilized within agar-agar and calcium alginate beads, respectively. The optimum pH (pH-10) of polygalacturonase was r...

Research paper thumbnail of Production Of 3-Hydroxypropanoic Acid Using Hydrogel Compartmentalized Microbial Strains

2nd International Conference on Biological Research and Applied Science

Research paper thumbnail of Production Of 3-Hydroxypropanoic Acid Using Hydrogel Compartmentalized Microbial Strains

2nd International Conference on Biological Research and Applied Science, Jan 22, 2022

Research paper thumbnail of Applications of Pectinolytic Enzymes in Process Industries

IntechOpen eBooks, May 17, 2023

Research paper thumbnail of Development of Pectinase Based Nanocatalyst by Immobilization of Pectinase on Magnetic Iron Oxide Nanoparticles Using Glutaraldehyde as Crosslinking Agent

Molecules

To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobili... more To increase its operational stability and ongoing reusability, B. subtilis pectinase was immobilized on iron oxide nanocarrier. Through co-precipitation, magnetic iron oxide nanoparticles were synthesized. Scanning electron microscopy (SEM) and energy dispersive electron microscopy (EDEX) were used to analyze the nanoparticles. Pectinase was immobilized using glutaraldehyde as a crosslinking agent on iron oxide nanocarrier. In comparison to free pectinase, immobilized pectinase demonstrated higher enzymatic activity at a variety of temperatures and pH levels. Immobilization also boosted pectinase’s catalytic stability. After 120 h of pre-incubation at 50 °C, immobilized pectinase maintained more than 90% of its initial activity due to the iron oxide nanocarrier, which improved the thermal stability of pectinase at various temperatures. Following 15 repetitions of enzymatic reactions, immobilized pectinase still exhibited 90% of its initial activity. According to the results, pectina...

Research paper thumbnail of Compartmentalization of Pectinase within Cellulose Hydrogel: An Efficient Technique to Enhance the Catalytic Properties of Pectinase for Industrial Applications

Austin Journal of Biotechnology & Bioengineering, 2021

Pectinase catalyze the breakdown of pectin polymer and widely has been used in different industri... more Pectinase catalyze the breakdown of pectin polymer and widely has been used in different industrial preparations such as fruit juice preparation, liquification and scarification of plant biomass as well as coffee and tea fermentation. In this study, the pectinase from Bacillus licheniformis was compartmentalized within cellulose beads hydrogel using encapsulation technique to make it reusable with easy recovery from reaction mixture. The compartmentalization improved catalytic properties of pectinase and ensured its reusability for continuous uses. It was observed that 5.0% cellulose concentration was enough to form stable cellulose hydrogel beads with retention of high relative of activity of pectinase. The hydrogel compartmentalization didn’t change the optima pH and temperature for maximum relative activity and both the hydrogel compartmentalized pectinase and free pectinase maximum relative at same pH and temperature but the hydrogel compartmentalization increased the stability ...

Research paper thumbnail of Degradation of complex carbohydrate: Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support

Research paper thumbnail of Encapsulation of pectinase within polyacrylamide gel: characterization of its catalytic properties for continuous industrial uses

Heliyon, 2020

Pectinase as a biocatalyst play a significant role in food and textile industries. In this study,... more Pectinase as a biocatalyst play a significant role in food and textile industries. In this study, the pectinase was immobilized by encapsulation within polyacrylamide gel to enhance its catalytic properties and ensure the reusability for continuous industrial processes. 9.5% acrylamide and 0.5% N, N′- methylenebisacrylamide concentration gave high percentage of pectinase immobilization yield within gel. The catalytic properties of immobilized pectinase was determined with comparison of soluble pectinase. The immobilization of pectinase within polyacrylamide gel didn't effect catalytic properties of pectinase and both the free and immobilized pectinase showed maximum pectinolytic activity at 45 °C and pH 10. The Michaelis-Menten kinetic behavior of pectinase was slightly changed after immobilization and immobilized pectinase showed somewhat higher Km and lower Vmax value as compared to soluble pectinase. Polyacrylamide gel encapsulation enhanced the thermal stability of pectinase...

Research paper thumbnail of Immobilization And Characterization Of Pectinase From Bacillus Species Using Different Supports

Research paper thumbnail of Role of Artemisia macrocephala as enzymes inhibitor in dementia and nociception! A pharmacological study

Pure and Applied Biology, 2016

Research paper thumbnail of Phytochemical analysis and antibacterial properties of Calotropis procera against bacterial phytopathogens

World Journal of Biology and Biotechnology

Calotropis procera, is known as crown flower or giant milkweed and belongs to the family Asclepia... more Calotropis procera, is known as crown flower or giant milkweed and belongs to the family Asclepiadacea. It has been traditionally used for various medicinal purposes. In the present study, the phytochemical analysis, antioxidant property, and antimicrobial activity of C. procera were evaluated. Methanol was used as a solvent for the extract preparation using soxhlet extraction. The extracts were subjected to the analysis of the different secondary bioactive metabolites. Furthermore, the antimicrobial activities of these extracts were determined against various pathogens. The qualitative analysis of plant extracts of leaves stems, and roots showed the presence of phenolic compounds, alkaloids, carbohydrates, glycosidic, protein, phytosterols, steroid, saponin, and flavonoid compounds. The leaf extract of C. procera plants inhibited 95% 2,2-diphenyl-1-picrylhydrazyl (DDPH) activity at 0.8 mg/mL Methanol extract of C. procera showed the maximum antibacterial and antifungal activities a...

Research paper thumbnail of Single step immobilization of CMCase within agarose gel matrix: Kinetics and thermodynamic studies

Colloids and Surfaces B: Biointerfaces

Research paper thumbnail of Utilization of different polymers for the improvement of catalytic properties and recycling efficiency of bacterial maltase

International Journal of Biological Macromolecules

Research paper thumbnail of Production of commercially important enzymes from Bacillus licheniformis KIBGE-IB3 using date fruit wastes as substrate

Journal of Genetic Engineering and Biotechnology

Research paper thumbnail of Xylan Deterioration Approach: Purification and catalytic behavior optimization of a novel β-1,4-D-xylanohydrolase from Geobacillus stearothermophilus KIBGE-IB29

Research paper thumbnail of Production of α-1,4-glucosidase from Bacillus licheniformis KIBGE-IB4 by utilizing sweet potato peel

Environmental Science and Pollution Research, 2016

In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable subs... more In the current study, sweet potato peel (Ipomoea batatas) was observed as the most favorable substrate for the maximum synthesis of α-1,4-glucosidase among various agro-industrial residues. Bacillus licheniformis KIBGE-IB4 produced 6533.0 U ml(-1) of α-1,4-glucosidase when growth medium was supplemented with 1% dried and crushed sweet potato peel. It was evident from the results that bacterial isolate secreted 6539.0 U ml(-1) of α-1,4-glucosidase in the presence of 0.4% peptone and meat extract with 0.1% yeast extract. B. licheniformis KIBGE-IB4 released 6739.0 and 7190.0 U ml(-1) of enzyme at 40 °C and pH 7.0, respectively. An improved and cost-effective growth medium design resulted 8590.0 U ml(-1) of α-1,4-glucosidase with 1.3-fold increase as compared to initial amount from B. licheniformis KIBGE-IB4. This enzyme can be used to fulfill the accelerating demand of food and pharmaceutical industries. Further purification and immobilization of this enzyme can also enhance its utility for various commercial applications. Graphical abstract Pictorial representation of maltase production from sweet potato peel.

Research paper thumbnail of Maltase entrapment approach as an efficient alternative to increase the stability and recycling efficiency of free enzyme within agarose matrix

Journal of the Taiwan Institute of Chemical Engineers, 2016

Research paper thumbnail of Polyacrylamide Gel-Entrapped Maltase: An Excellent Design of Using Maltase in Continuous Industrial Processes

Applied Biochemistry and Biotechnology, 2016

Bacterial maltase catalyzes the hydrolysis of maltose and is known as one of the most significant... more Bacterial maltase catalyzes the hydrolysis of maltose and is known as one of the most significant hydrolases. It has several applications in different industrial processes but widely used in food fermentation technology and alcohol production. In the current study, entrapment technique was comprehensively examined using polyacrylamide gel as a matrix support to improve the stability and catalytic efficiency of maltase for continuous use. Maximum entrapment yield of maltase was achieved at 10 % polyacrylamide concentration with 3.0-mm bead size. Optimized conditions indicated an increase in the reaction temperature from 45 to 55 °C after maltase entrapment while no change was observed in the reaction time and pH. An increase in the K m value of entrapped maltase was attained whereas V max value decreased from 8411.0 to 6813.0 U ml(-1) min(-1) with reference to its free counterpart. Entrapped maltase showed remarkable thermal stability and retained 16 % activity at 70 °C even after 120.0 min. Entrapped maltase also exhibited excellent recycling efficiency up to eight consecutive reaction cycles. With respect to economic feasibility, entrapped maltase indicates its high potential to be used in various biotechnological applications.

Research paper thumbnail of The Biology of Balochistani Weed: Cyperus rotundus Linnaeus. A Review

Pure and Applied Biology, 2015

Research paper thumbnail of Continuous degradation of maltose by enzyme entrapment technology using calcium alginate beads as a matrix

Biochemistry and Biophysics Reports, 2015

Research paper thumbnail of Immobilization of Pectin Depolymerising Polygalacturonase Using Different Polymers

International journal of biological macromolecules, Jan 7, 2015

Polygalacturonase catalyses the hydrolysis of pectin substances and widely has been used in food ... more Polygalacturonase catalyses the hydrolysis of pectin substances and widely has been used in food and textile industries. In current study, different polymers such as calcium alginate beads, polyacrylamide gel and agar-agar matrix were screened for the immobilization of polygalacturonase through entrapment technique. Polyacrylamide gel was found to be most promising one and gave maximum (89%) immobilization yield as compared to agar-agar (80%) and calcium alginate beads (46%). The polymers increased the reaction time of polygalacturonase and polymers entrapped polygalacturonases showed maximum pectinolytic activity after 10minutes of reaction as compared to free polygalacturonase which performed maximum activity after 5.0minutes of reaction time. The temperature of polygalacturonase for maximum enzymatic activity was increased from 45°C to 50°C and 55°C when it was immobilized within agar-agar and calcium alginate beads, respectively. The optimum pH (pH-10) of polygalacturonase was r...