Immobilization of Serratia plymuthica by ionic gelation and cross-linking with transglutaminase for the conversion of sucrose into isomaltulose

Carvalho, Priscila Hoffmann; Kawaguti, Haroldo Yukio; Souza, Weysser Felipe Cândido de; Sato, Hélia Harumi

doi:10.1007/s00449-021-02513-x

Cited by 10 publications

(2 citation statements)

References 36 publications

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“…The optimal experimental conditions determined were as follows: 1.7% sodium alginate, 0.25 mol/L CaCl 2 , 0.5% gelatin, 3.5% transglutaminase, and 33.5% cell aggregates. These conditions effectively improved cell immobilization and the efficiency of converting sucrose to isomaltulose, resulting in a yield of isomaltulose reaching 71.04% [49]. Souza et al also used alginate-gelatin to embed Erwinia sp.…”

Section: Embedding Methodsmentioning

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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Section: Embedding Methodsmentioning

confidence: 99%

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

Jing,

Hou,

et al. 2024

Foods

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show abstract

“… Glucose oxidase Aspergillus Niger Alginate Encapsulation NA NA Retained 92% of activity at pH 4.0 and reused up to 7 cycles Reduction of fermentable sugar in the must [ 133 ] 15. Transglutaminase Serratia plymuthica Alginate Cross-linking NA NA Enhanced stability and isomaltulose yield Sucrose conversion into isomaltulose [ 134 ] 16. Pectinase Aspergillus aculeatus Calcium alginate beads Entrapment 16.45 6.07 Excellent operational stability retained 80% of activity up to three cycles of reuse Fruit juice clarifiation [ 135 ] 18.…”

Section: Polymeric Matrices Immobilized Enzymes For Industrial Bio-ca...mentioning

confidence: 99%

Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications

et al. 2022

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Enzymes of commercial importance, such as lipase, amylase, laccase, phytase, carbonic anhydrase, pectinase, maltase, glucose oxidase etc ., show multifunctional features and have been extensively used in several fields including fine chemicals, environmental, pharmaceutical, cosmetics, energy, food industry, agriculture and nutraceutical etc . The deployment of biocatalyst in harsh industrial conditions has some limitations, such as poor stability. These drawbacks can be overcome by immobilizing the enzyme in order to boost the operational stability, catalytic activity along with facilitating the reuse of biocatalyst. Nowadays, functionalized polymers and composites have gained increasing attention as an innovative material for immobilizing the industrially important enzyme. The different types of polymeric materials and composites are pectin, agarose, cellulose, nanofibers, gelatin, and chitosan. The functionalization of these materials enhances the loading capacity of the enzyme by providing more functional groups to the polymeric material and hence enhancing the enzyme immobilization efficiency. However, appropriate coordination among the functionalized polymeric materials and enzymes of interest plays an important role in producing emerging biocatalysts with improved properties. The optimal coordination at a biological, physical, and chemical level is requisite to develop an industrial biocatalyst. Bio-catalysis has become vital aspect in pharmaceutical and chemical industries for synthesis of value-added chemicals. The present review describes the current advances in enzyme immobilization on functionalized polymers and composites. Furthermore, the applications of immobilized enzymes in various sectors including bioremediation, biosensor and biodiesel are also discussed.

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Sequential optimization strategy for the immobilization of Erwinia sp. D12 cells and the production of isomaltulose with high stability and prebiotic potential

Souza

Castro

Sato

2022

Bioprocess Biosyst Eng

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Immobilization of Serratia plymuthica by ionic gelation and cross-linking with transglutaminase for the conversion of sucrose into isomaltulose

Cited by 10 publications

References 36 publications

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

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

Mechano-chemical and biological energetics of immobilized enzymes onto functionalized polymers and their applications

Sequential optimization strategy for the immobilization of Erwinia sp. D12 cells and the production of isomaltulose with high stability and prebiotic potential

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