Recent innovations in immobilization of β-galactosidases for industrial and therapeutic applications

Duan, Feiyu; Sun, Tong; Zhang, Jingwen; Wang, Ke; Wen, Yan; Lu, Lili

doi:10.1016/j.biotechadv.2022.108053

Cited by 17 publications

(6 citation statements)

References 155 publications

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“…There is a growing interest in the development of effective supports for immobilizing β-galactosidase, given its significance in various industries. While carbon nanotubes and inorganic supports, particularly nanomaterials like nanodiamonds, ZnO nanoparticles, SiO 2 nanoparticles, and silver nanoparticles, have been utilized for this purpose due to their remarkable mechanical properties [45][46][47][48][49][50][51], the recent trend favors the use of polymeric supports. This preference is attributed to the abundance of polymeric materials, their versatility, and biocompatibility, offering promising prospects for β-galactosidase immobilization.…”

Section: Methods Of Enzyme Immobilizationmentioning

confidence: 99%

Hydrolysis of Lactose: Conventional Techniques and Enzyme Immobilization Strategies on Polymeric Supports

Lucas Vallejo-García,

Cutillo-Foraster,

Arnaiz

et al. 2024

Milk Proteins - Technological Innovations, Nutrition, Sustainability and Novel Applications [Working Title]

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This chapter explores lactose hydrolysis, emphasizing conventional techniques and the noteworthy immobilization of β-galactosidase on polymeric matrices to enhance the process. Lactose, present in milk and dairy, poses challenges for lactose-intolerant individuals, requiring enzymatic hydrolysis for lactose-free product development. The presence of other milk components, such as proteins and minerals, can indirectly influence the efficiency of lactose hydrolysis by potentially interacting with β-galactosidase enzyme or affecting its stability and activity, making it necessary to control factors such as enzyme concentration, temperature, pH, and reaction time to improve lactose hydrolysis rates. The chapter delves into established methodologies, covering enzymatic kinetics, reaction conditions, and substrate concentrations. It also describes the innovative approach of immobilizing β-galactosidase on polymeric supports to enhance enzyme stability, reusability, and overall efficiency in lactose hydrolysis. Discussions include the design of suitable polymeric matrices, providing insights into mechanisms governing catalytic performance. This comprehensive exploration contributes to understanding lactose hydrolysis, offering valuable insights for developing efficient and sustainable enzymatic processes applicable to the food and pharmaceutical industries.

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Section: Methods Of Enzyme Immobilizationmentioning

confidence: 99%

Hydrolysis of Lactose: Conventional Techniques and Enzyme Immobilization Strategies on Polymeric Supports

Lucas Vallejo-García,

Cutillo-Foraster,

Arnaiz

et al. 2024

Milk Proteins - Technological Innovations, Nutrition, Sustainability and Novel Applications [Working Title]

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“…Since the new century, the development of materials science has provided a broad development space for immobilized enzyme carriers. The emergence of graphene oxide, magnetic materials, metal-organic frameworks, and membrane materials has provided new opportunities for the development of immobilized enzyme carriers and immobilization technologies [84].…”

Section: Novel Materialsmentioning

confidence: 99%

A Critical Review on Immobilized Sucrose Isomerase and Cells for Producing Isomaltulose

Jing,

Hou,

et al. 2024

Foods

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Isomaltulose is a novel sweetener and is considered healthier than the common sugars, such as sucrose or glucose. It has been internationally recognized as a safe food product and holds vast potential in pharmaceutical and food industries. Sucrose isomerase is commonly used to produce isomaltulose from the substrate sucrose in vitro and in vivo. However, free cells/enzymes were often mixed with the product, making recycling difficult and leading to a significant increase in production costs. Immobilized cells/enzymes have the following advantages including easy separation from products, high stability, and reusability, which can significantly reduce production costs. They are more suitable than free ones for industrial production. Recently, immobilized cells/enzymes have been encapsulated using composite materials to enhance their mechanical strength and reusability and reduce leakage. This review summarizes the advancements made in immobilized cells/enzymes for isomaltulose production in terms of refining traditional approaches and innovating in materials and methods. Moreover, innovations in immobilized enzyme methods include cross-linked enzyme aggregates, nanoflowers, inclusion bodies, and directed affinity immobilization. Material innovations involve nanomaterials, graphene oxide, and so on. These innovations circumvent challenges like the utilization of toxic cross-linking agents and enzyme leakage encountered in traditional methods, thus contributing to enhanced enzyme stability.

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“…Molecular dynamics simulations were carried out using the AMBER software package (version 18) [52,53]; with the ff14SB force field [54], using its GPU-accelerated pmemd.cuda utility during equilibration and production, and sander otherwise [55]. Simulations employed the experimental crystal structure of M-GH1; residues were modeled in their standard protonation states at physiological pH, as predicted by PROPKA, version 3.2 [56]: this resulted in Glu171 side chain being protonated and His residues 8,126,132,185,200,206,303,343, 435 being protonated on Nε2, and His 64,65, 201, 381 being protonated on Nδ1. Hydrogen atoms were added using the tleap utility in AMBERTOOLS (version 19) [52].…”

Section: Simulationsmentioning

confidence: 99%

Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1

Gourlay,

Mangiagalli,

Moroni

et al. 2024

The FEBS Journal

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Cold‐active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that very diverse structural and functional changes are exploited in different protein families and within the same family. In this context, we studied the cold adaptation mechanism and the functional properties of a member of the glycoside hydrolase family 1 (GH1) from the Antarctic bacterium Marinomonas sp. ef1. This enzyme exhibits all typical functional hallmarks of cold adaptation, including high catalytic activity at 5 °C, broad substrate specificity, low thermal stability, and higher lability of the active site compared to the overall structure. Analysis of the here‐reported crystal structure (1.8 Å resolution) and molecular dynamics simulations suggest that cold activity and thermolability may be due to a flexible region around the active site (residues 298–331), whereas the dynamic behavior of loops flanking the active site (residues 47–61 and 407–413) may favor enzyme‐substrate interactions at the optimal temperature of catalysis (Topt) by tethering together protein regions lining the active site. Stapling of the N‐terminus onto the surface of the β‐barrel is suggested to partly counterbalance protein flexibility, thus providing a stabilizing effect. The tolerance of the enzyme to glucose and galactose is accounted for by the presence of a “gatekeeping” hydrophobic residue (Leu178), located at the entrance of the active site.

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Recent innovations in immobilization of β-galactosidases for industrial and therapeutic applications

Cited by 17 publications

References 155 publications

Hydrolysis of Lactose: Conventional Techniques and Enzyme Immobilization Strategies on Polymeric Supports

Hydrolysis of Lactose: Conventional Techniques and Enzyme Immobilization Strategies on Polymeric Supports

A Critical Review on Immobilized Sucrose Isomerase and Cells for Producing Isomaltulose

Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1

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