Surfaces Coated with Polymer Brushes Work as Carriers for Histidine Ammonia Lyase

TY - JOUR

T1 - Surfaces Coated with Polymer Brushes Work as Carriers for Histidine Ammonia Lyase

AU - Marcelino, Thaís

AU - Docampo, Miguel A Ramos

AU - Qian, Xiaomin

AU - Ade, Carina

AU - Brodszkij, Edit

AU - Ceccato, Marcel

AU - Foss, Morten

AU - Dulchavsky, Mark

AU - Bardwell, James C A

AU - Städler, Brigitte

PY - 2023/8

Y1 - 2023/8

N2 - The immobilization of enzymes on solid supports is an important challenge in biotechnology and biomedicine. In contrast to other methods, enzyme deposition in polymer brushes offers the benefit of high protein loading that preserves enzymatic activity in part due to the hydrated 3D environment that is available within the brush structure. The authors equipped planar and colloidal silica surfaces with poly(2-(diethylamino)ethyl methacrylate)-based brushes to immobilize Thermoplasma acidophilum histidine ammonia lyase, and analyzed the amount and activity of the immobilized enzyme. The poly(2-(diethylamino)ethyl methacrylate) brushes are attached to the solid silica supports either via a "grafting-to" or a "grafting-from" method. It is found that the grafting-from method results in higher amounts of deposited polymer and, consequently, higher amounts of Thermoplasma acidophilum histidine ammonia lyase. All polymer brush-modified surfaces show preserved catalytic activity of the deposited Thermoplasma acidophilum histidine ammonia lyase. However, immobilizing the enzyme in polymer brushes using the grafting-from method resulted in twice the enzymatic activity from the grafting-to approach, illustrating a successful enzyme deposition on a solid support.

AB - The immobilization of enzymes on solid supports is an important challenge in biotechnology and biomedicine. In contrast to other methods, enzyme deposition in polymer brushes offers the benefit of high protein loading that preserves enzymatic activity in part due to the hydrated 3D environment that is available within the brush structure. The authors equipped planar and colloidal silica surfaces with poly(2-(diethylamino)ethyl methacrylate)-based brushes to immobilize Thermoplasma acidophilum histidine ammonia lyase, and analyzed the amount and activity of the immobilized enzyme. The poly(2-(diethylamino)ethyl methacrylate) brushes are attached to the solid silica supports either via a "grafting-to" or a "grafting-from" method. It is found that the grafting-from method results in higher amounts of deposited polymer and, consequently, higher amounts of Thermoplasma acidophilum histidine ammonia lyase. All polymer brush-modified surfaces show preserved catalytic activity of the deposited Thermoplasma acidophilum histidine ammonia lyase. However, immobilizing the enzyme in polymer brushes using the grafting-from method resulted in twice the enzymatic activity from the grafting-to approach, illustrating a successful enzyme deposition on a solid support.

KW - X-ray photoelectron spectroscopy

KW - enzymes

KW - histidine ammonia lyase

KW - poly(2-(diethylamino)ethyl methacrylate)

KW - polymer brushes

KW - silica particles

KW - stability

KW - Methacrylates/chemistry

KW - Silicon Dioxide

KW - Histidine Ammonia-Lyase

KW - Polymers/chemistry

U2 - 10.1002/mabi.202200528

DO - 10.1002/mabi.202200528

M3 - Journal article

C2 - 36971346

SN - 1616-5187

VL - 23

JO - Macromolecular Bioscience

JF - Macromolecular Bioscience

IS - 8

M1 - 2200528

ER -