Overviewing the Application of β-Galactosidase “Immobilized on Nanoparticles” in Dairy Industries

Alshanberi, Asim Muhammed; Al-Shaeri, Majed Ahmed; Ansari, Shakeel Ahmed

doi:10.1590/1678-4324-2021180747

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Sumário

Review - Agriculture, Agribusiness and Biotechnology • Braz. arch. biol. technol. 64 • 2021 • https://doi.org/10.1590/1678-4324-2021180747 copy

Overviewing the Application of β-Galactosidase “Immobilized on Nanoparticles” in Dairy Industries

Authorship SCIMAGO INSTITUTIONS RANKINGS

HIGHLIGHTS

Nanoparticles (NPs) exhibited greater performance of immobilized enzyme.

They influence the sensitivity, selectivity, loading, mobility and stability of enzymes.

β-galactosidase immobilized on NPs retained greater activity against various physical and chemical denaturants.

Abstract

Owing to the excellent catalytic potential, β-galactosidase (EC: 3.2.1.23) has been exploited as an important industrial enzyme for obtaining galactooligosaccharides (GOS) and lactose-free products in dairy industries. Moreover, novel technologies have been implemented in the recent past for preparing and modifying nanoparticles (NPs) for immobilizing therapeutically and industrially important enzymes. Nanoparticles based enzyme immobilization (NBEI) offered more stability and robustness to the enzymes due to their fixed conformation and hence extend their applications in broader areas. A quick overview of the results exhibited greater activity for the enzymes immobilized on NPs as compared to enzyme immobilized on 2-D matrices. Based on these findings, this review was aimed to emphasize the recent development achieved for immobilizing β-galactosidase on NPs with their specific utilization in obtaining dairy products. These studies includes β-galactosidases from various sources that were immobilized on various NPs for hydrolyzing lactose in batch and continuous reactors, and for the production of GOS in biotechnology industries. NBEI of β-galactosidase offered profound stability for transporting substrate and product for enzymatic reactions, apart from cost effective advantage due to reusable nature of immobilized enzyme.

Keywords:
β-galactosidase; immobilized nanobiocatalyst; dairy industries; nanoparticles; surface modification

Source of β- galactosidase	Nanoparticles used for immobilization	Efficiency	Biotechnological applications	Reference
Lactobacillus plantarum HF571129	ZnO	The rate of lactose hydrolysis was 0.023 and 0.04 per min. t_1/2 was 30.13 and 17.325 min for batch and packed bed, respectively.	Lactose hydrolysis	24
Aspergillus oryzae	Fe₃O₄-chitosan nanoparticles	Bioconversion determined by these nanocarriers showed 59 % yield.	GOS production	25
Aspergillus oryzae	ZnO	Maximum lactose hydrolysis obtained by ZnO-NPs-β galactosidase was 71% in 8 h.	Lactose hydrolysis from whey and milk	26
Aspergillus oryzae	Graphene-iron oxide nanocomposites	Genotoxicity assay revealed that this system exhibited negligible toxicity to pBR322 DNA plasmid and human lymphocytes.	Construction of biosensors, production of lactose-free dairy products and large scale enzyme catalyzed applications	27
Aspergillus oryzae	Chitosan	Hydrolysis was over 80% even after 50 cycles of reuse.	Lactose hydrolysis	28
Agaricus bisporus	Polyaniline nanofiber, DEAE cellulose fiber, CM cellulose fiber and polystyrene nanofiber	PANI-, PAMP-, and DEAE-lactase exhibited greater percentage of lactose conversion (100%, 47% and 12%, respectively).	Lactose hydrolysis	29
Aspergillus oryzae	Core-shell silica nanoparticles	After nine cycles of hydrolytic reaction, the encapsulated β-galactosidase retained 94% of its initial activity.	Lactose hydrolysis	30

Source of β-galactosidase	NPs	Ligand	Efficiency	Application	Reference
Kluyveromyces lactis	Al₂O₃	Concanavalin A	Comet assay exhibited negligible change in tail length of comet after treating the lymphocytes with nanosupport.	Biomedical/ biotechnological industries	35
Aspergillus oryzae	ZnO	Concanavalin A	No significant change was observed in the band intensity of pUC19 plasmid upon nanosupport treatment.	Biomedical/biotechnological/biosensors	36
Aspergillus oryzae	Magnetic nanoparticles	Amine	Ability to hydrolyze substrates during multiple cycles of use.	Continuous production of lactose hydrolyzed products	37
Kluyveromyces lactis	Multi-walled carbon nanotubes	Glutaraldehyde	Functionalized MWCNTs retained greater biocatalytic activity at higher concentration of galactose.	Lactose biosensors	39
Aspergillus oryzae	Nanodiamonds	Glutaraldehyde	Modified NDs retained 7420 U/gm enzyme and exhibited improved lactolysis in batch processes even after 10 h.	Hydrolysis of lactose from solution in batch processes	40
Aspergillus oryzae	AgNPs	Nitric acid/sulfuric acid	Immobilized enzyme yielded greater amount of galacto-oligosaccharides at higher temperatures from 0.1 mol/L lactose solution at pH 4.5	GOS production	41
Aspergillus oryzae	AgNPs	Glutaraldehyde	The remarkable bioconversion rates of lactose promoting its use in producing lactose-free dairy products.	Production of lactose free dairy products in batch reactors	42
Aspergillus oryzae	Graphene	Ethanol	Maximum GOS content registered an increase in lactose conversion.	GOS production	43
Aspergillus oryzae	Agarose nanoparticles	Galactose	The developed nanosystem hydrolyzed greater amount of lactose at higher temperatures, thereby suggesting its application in large scale dairy industries.	Production of lactose-free dairy products at large scale	44
Kluyveromyces lactis	Silicon dioxide	Glutaraldehyde	Maximum lactose hydrolysis by immobilized enzyme was achieved after 8 h.	Bioremediation for cleaning and converting whey into value added products	45
Aspergillus oryzae	Silica nanoparticles	Glutaraldehyde	The rate of lactose and whey hydrolysis by immobilized enzyme was 1.5 and 2.5 times higher as compared to the free enzyme, respectively	Lactose and whey hydrolysis	46
Aspergillus oryzae	Fe₃O₄-NPs	Chitosan	Maximum GOS yield was observed as 50.5% from 36% w/v lactose on a dry weight basis.	GOS production	47
Aspergillus oryzae	Cobalt/ Multi-walled carbon nanotubes	Polyaniline	The bound enzyme retained 92% activity after its 10^th repeated, and negligible change in the band intensity of pBR322 plasmid.	Biosensors	48

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[1] *Correspondence: shakeel.ansari@bmc.edu.sa(S.A.A.).