Abstract:Cyclodextrin (CD) is a non-reducing maltooligosaccharides which able to form inclusion complexes with many hydrophobic molecules, changing their physical and chemical properties. With these properties, CD has been discovered to have numerous applications in food industries, pharmaceutical, agricultural and environmental engineering. CD is produced by the enzymatic reaction between cyclodextrin glucanotransferase (CGTase) and starch. Various enzyme immobilization techniques such as adsorption, entrapment, encap… Show more
“…This contributes to greater rigidity in enzymatic structure and, in turn, higher catalytic activity and saccharification efficiency. However, a longer time has been found to decrease the efficiency of immobilization procedures and incur higher costs. , Besides, the duration has to be judiciously decided: in one study on immobilizing cellulase onto electrospun polyacrylonitrile (PAN) nanofibrous membranes, a 30 min immobilization time was found optimum whereas an overly prolonged time impaired the specific activity of enzyme due to protein denaturation …”
Section: Influence Of Immobilization Operating Conditions
On Enzymati...mentioning
Lignocellulosic biomass (LCB), the most abundant natural
polymer
across the globe, offers much potential to be a sustainable, non-food-competing
carbon source for the production of biofuels and biochemicals. Compared
to chemical hydrolysis, enzymatic saccharification of LCB is commonly
regarded as less energy-intensive, less toxic, and more environment-benign
for efficient, targeted sugar recovery. Nonetheless, the sensitivity
of enzymes toward denaturing conditions, poor recyclability, and costs
are the bottlenecks for their industrial application. Accordingly,
enzyme immobilization has been proposed to address such shortcomings.
This review appraises the type of support matrices and enzyme-immobilization
techniques,
and examines various factors impacting the enzyme immobilization to
identify the optimal technique for LCB conversion. Covalent binding
of enzymes onto magnetic nanoparticles has been suggested as an excellent
immobilization technique in terms of good reusability and improved
system stability across changing pH and temperatures. State-of-the-art
challenges and future research directions on the enzymatic saccharification
of LCB are discussed.
“…This contributes to greater rigidity in enzymatic structure and, in turn, higher catalytic activity and saccharification efficiency. However, a longer time has been found to decrease the efficiency of immobilization procedures and incur higher costs. , Besides, the duration has to be judiciously decided: in one study on immobilizing cellulase onto electrospun polyacrylonitrile (PAN) nanofibrous membranes, a 30 min immobilization time was found optimum whereas an overly prolonged time impaired the specific activity of enzyme due to protein denaturation …”
Section: Influence Of Immobilization Operating Conditions
On Enzymati...mentioning
Lignocellulosic biomass (LCB), the most abundant natural
polymer
across the globe, offers much potential to be a sustainable, non-food-competing
carbon source for the production of biofuels and biochemicals. Compared
to chemical hydrolysis, enzymatic saccharification of LCB is commonly
regarded as less energy-intensive, less toxic, and more environment-benign
for efficient, targeted sugar recovery. Nonetheless, the sensitivity
of enzymes toward denaturing conditions, poor recyclability, and costs
are the bottlenecks for their industrial application. Accordingly,
enzyme immobilization has been proposed to address such shortcomings.
This review appraises the type of support matrices and enzyme-immobilization
techniques,
and examines various factors impacting the enzyme immobilization to
identify the optimal technique for LCB conversion. Covalent binding
of enzymes onto magnetic nanoparticles has been suggested as an excellent
immobilization technique in terms of good reusability and improved
system stability across changing pH and temperatures. State-of-the-art
challenges and future research directions on the enzymatic saccharification
of LCB are discussed.
Enzyme immobilization on inorganic materials is gaining more attention with the potential characteristics of high-surface-area-to-volume ratios, increasing the efficiency of enzyme loading on the support. Metal oxide hybrid support was prepared by a wetness impregnation of five metal precursors, including CaO, CuO, MgO, NiO, and ZnO, on Al2O3 and used as a support for the immobilization of Candida rugosa lipase (CRL) by adsorption. Maximum activity recovery (70.6%) and immobilization efficiency (63.2%) were obtained after optimization of five parameters using response surface methodology (RSM) by Box–Behnken design (BBD). The biochemical properties of immobilized CRL showed high thermostability up to 70 °C and a wide range in pH stability (pH 4–10). TGA-DTA and FTIR analysis were conducted, verifying thermo-decomposition of lipase and the presence of an amide bond. FESEM-EDX showed the homogeneous distribution and high dispersion of magnesium and CRL on MgO-Al2O3, while a nitrogen adsorption–desorption study confirmed MgO-Al2O3 as a mesoporous material. CRL/MgO-Al2O3 can be reused for up to 12 cycles and it demonstrated high tolerance in solvents (ethanol, isopropanol, methanol, and tert-butanol) compared to free CRL.
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