scholarly journals Immobilization of Aspergillus oryzae  β-Galactosidase on Cellulose Acetate-Polymethylmethacrylate Membrane and Its Application in Hydrolysis of Lactose from Milk and Whey

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Shakeel Ahmed Ansari ◽  
Rukhsana Satar ◽  
Syed Kashif Zaidi ◽  
Abrar Ahmad
Keyword(s):  
Cellulose Acetate ◽  
Aspergillus Oryzae ◽  
Immobilized Enzyme ◽  
Product Inhibition ◽  
Lactose Hydrolysis ◽  
Batch Reactors ◽  
Maximum Reaction Rate ◽  
Maximum Reaction ◽  
Repeated Use ◽  
Physical And Chemical

The present study demonstrates the immobilization of Aspergillus oryzae β-galactosidase on cellulose acetate-polymethylmethacrylate (CA-PMMA) membrane and its application in hydrolyzing lactose in dairy industries. The effect of physical and chemical denaturants like pH, temperature, product inhibition by galactose, storage stability, and reuse number of the enzyme immobilized on CA-PMMA membrane has been investigated. Lactose was hydrolyzed from milk and whey in batch reactors at 50°C by free and immobilized β-galactosidase (IβG). Optimum pH for the free and immobilized enzyme was found to be the same, that is, 4.5. However, IβG retained greater fractions of catalytic activity at lower and higher pH ranges. The temperature optimum for the immobilized enzyme was increased by 10°C. Moreover, Michaelis-Menten constant was increased for IβG as compared to the native one while maximum reaction rate was reduced for the immobilized enzyme. The preserved activity of free and immobilized enzyme was found to be 45% and 83%, respectively, after five weeks of storage at 4°C. Reusability of IβG was observed to be 86% even after fifth repeated use, thereby signifying its application in lactose hydrolysis (as shown in lab-scale batch reactors) in various dairy products including milk and whey.

scholarly journals Validation and Optimization of Polyvinyl Alcohol-Functionalized Gold Nanoparticles for Producing Lactose-Free Dairy Products

2021 ◽  
Vol 37 (3) ◽  
pp. 643-647
Author(s):  
Asim Muhammed Alshanberi ◽  
Shakeel Ahmed Ansari
Keyword(s):  
Gold Nanoparticles ◽  
Polyvinyl Alcohol ◽  
Dairy Products ◽  
Biomedical Applications ◽  
Immobilized Enzyme ◽  
Kluyveromyces Lactis ◽  
Lactose Hydrolysis ◽  
Batch Reactors ◽  
Stable Matrix ◽  
Functionalized Aunps

The present study demonstrates the synthesis of lactose-free dairy items by Kluyveromyces lactis β-galactosidase bound to polyvinyl alcohol (PVA)-modified gold nanoparticles (AuNPs). The size of AuNPs was analyzed by dynamic light scattering experiment. The developed AuNPs served as a stable matrix for enzyme immobilization which was observed by obtaining 88% immobilization yield. Km and Vmax were determined for soluble and immobilized enzyme by incubating them with varying concentrations of substrate. Our findings demonstrated that immobilization leads to an increase of Km and a decline in Vmax values for the enzyme attached to PVA-functionalized AuNPs. Moreover, the enzyme conjugated to surface functionalized AuNPs displayed exceptional conversion of lactose hydrolysis in batch reactors at 40 oC in contrast to its hydrolysis at 50 oC. Hence, the developed nanosystem [β-galactosidase-(PVA-modified AuNPs)] serves as an excellent model for suggesting its application in other biomedical applications, particularly for constructing lactose based biosensors.

Improvement of the Activity of Naringinase by Covalent Immobilization on Sodium Alginate in Biomaterial Engineering and its Applications

2012 ◽  
Vol 578 ◽  
pp. 187-190 ◽  
Author(s):  
Sheng Jiao Lei ◽  
Si Yi Pan
Keyword(s):  
Sodium Alginate ◽  
Immobilized Enzyme ◽  
Promising Result ◽  
Covalent Immobilization ◽  
Future Application ◽  
Optimal Conditions ◽  
Michaelis Constant ◽  
Maximum Reaction ◽  
Repeated Use ◽  
Effects Of Temperature

Naringinase using different methods to immobilize in alginate sodium have been studied. The results showed that adopting 3% sodium alginate as carrier and using the method of covalent immobilization through 2.0% glutaraldehyde were optimized. The retained activity of immobilized naringinase could reach 129.64% under optimal conditions. Moreover, the retained activity of immobilized naringinase increases with decreasing concentration of naringinase solution. This is a promising result of lowering production cost for future application of immobilized naringinase in biomaterial engineering. On seven consecutive repeated use of immobilized naringinase, 90% retained activity were observed. Michaelis constant (Km) and maximum reaction velocity (Vm) were calculated for the free and immobilized enzyme systems. Effects of temperature and pH on enzyme activity were estimated.

scholarly journals Future Applications of Apricot (Prunus Armeniaca Kaisa) ß Galactosidase in Dairy Industry

2014 ◽  
Vol 16 (3) ◽  
pp. 74-79 ◽  
Author(s):  
Shakeel Ahmed Ansari ◽  
Rukhsana Satar ◽  
Syed Kashif Zaidi ◽  
Mohd Jahir Khan ◽  
Muhammad Imran Naseer ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Dairy Products ◽  
Immobilized Enzyme ◽  
Prunus Armeniaca ◽  
Batch Processes ◽  
Lactose Hydrolysis ◽  
Initial Activity ◽  
Temperature Optimum ◽  
Repeated Use ◽  
Hydrolysis Of

Abstract The present study demonstrates the immobilization of β galactosidase from apricots (Prunus armeniaca kaisa) on an inexpensive concanavalin A layered cellulose-alginate hybrid gel. Immobilized β galactosidase retained 78% of the initial activity after crosslinking by glutaraldehyde. It exhibited greater fraction of activity at both acidic and basic pH, and showed broad spectrum temperature optimum as compared to free enzyme. Moreover, immobilized enzyme exhibited higher thermal stability at 60°C and retained 80% of the original enzyme activity in presence of 3% galactose. The crosslinked immobilized enzyme showed improved hydrolysis of lactose from milk and whey in batch processes at 50°C as well as in continuous reactors operated at fl ow rate of 20 mL/h and 30 mL/h even after one month. Moreover, crosslinked adsorbed β galactosidase retained 76% activity even after its sixth repeated use, thereby promoting its use for lactose hydrolysis in various dairy products even for longer durations.

Formation of composite gel fiber from cellulose acetate and zirconium tetra-n-butoxide and entrap-immobilization of β-galactosidase on the fiber

2003 ◽  
Vol 18 (3) ◽  
pp. 672-676 ◽  
Author(s):  
K. Nakane ◽  
T. Ogihara ◽  
N. Ogata ◽  
Y. Kurokawa
Keyword(s):  
Cellulose Acetate ◽  
Fiber Diameter ◽  
Fiber Surface ◽  
Lactose Hydrolysis ◽  
Phosphate Solution ◽  
Michaelis Constant ◽  
Coordination Numbers ◽  
Maximum Reaction ◽  
Composite Gel ◽  
Opposite Tendency

The formation of a composite gel fiber from cellulose acetate and zirconium tetra-n-butoxide was examined. The gel was thought to have formed by the coordination of OH and CO groups of cellulose to zirconium, taking six coordination numbers around the zirconium. The gel fiber had good stability in common solvents, phosphate solution, and electrolyte solution. Then, under mild conditions, a β-galactosidase was entrap-immobilized on it. The apparent Michaelis constant of the Immobilized β-galactosidase was larger than that of native β-galactosidase, whereas the opposite tendency was observed for the maximum reaction velocity. The activity of the immobilized β-galactosidase increased as the fiber diameter decreased. These findings indicated that lactose hydrolysis took place in the vicinity of the fiber surface. The immobilized β-galactosidase had a higher thermal stability than the native type.

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