A magnetic tri-enzyme nanobiocatalyst for fruit juice clarification

Sojitra, Uttam V.; Nadar, Shamraja S.; Rathod, Virendra K.

doi:10.1016/j.foodchem.2016.06.074

Cited by 116 publications

(46 citation statements)

References 37 publications

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“…As the pumpkin‐hawthorn compound juice contains high a content of pectin and starch, it can be expected that the use of I‐PG for the clarification of such juice is more efficient when compared to the use of only immobilized pectinase or glucoamylase on the same carriers as I‐PG. It has been reported that a tri‐enzyme (pectinase, α‐amylase, and cellulose) magnetic biocatalyst reduced a turbidity of grape, apple, and pineapple juices more efficiently than the mixture of individually immobilized enzymes (Sojitra et al, ). We believe that the same enhancement occurs with the matrix‐bound enzymes described in this work.…”

Section: Resultsmentioning

confidence: 99%

“…Numerous works regarding the immobilization of polysaccharide-hydrolyzing enzymes, such as pectinase (Chauhan, Vohra, Lakhanpal, & Gupta, 2015;Rajdeo et al, 2016;Ramírez Tapias, Rivero, Gallego, Guisán, & Trelles, 2016), α-amylase (Carrin et al, 2004), glucoamylase (Salgaonkar, Nadar, & Rathod, 2018), onto various supports and their application in food industry have been reported. In particular, an investigation on the co-immobilization of three enzymes (pectinase, α-amylase and cellulose) and the subsequent influence on juice clarification has also been reported (Sojitra, Nadar, & Rathod, 2016).…”

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confidence: 99%

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Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

et al. 2018

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Co‐immobilization of pectinase and glucoamylase onto sodium alginate/graphene oxide beads was achieved by N,N′‐dicyclohexylcarbodiimide/N‐hydroxysuccinimide as activating agent. The co‐immobilized pectinase‐glucoamylase (I‐PG) prepared under optimal conditions (pH 4.0, 40°C and 35 min) possessed pectinase activity of 1,227.5 ± 36.5U/g and glucoamylase activity of 1,027.2 ± 29.2U/g, with activity recovery of 73.8% and 85.2%, respectively. Both pectinase and glucoamylase in I‐PG possessed wider pH tolerance and superior thermal stability to those of their free counterparts. Reusability studies indicated that both enzymes in I‐PG retained over 60% of initial activity after six times of reuse. Conditions for the hydrolysis of the pumpkin–hawthorn compound juice by I‐PG were optimized using orthogonal experiments. After treatment with I‐PG, light transmittance, soluble solids, and reducing sugar content in the resulting juice increased significantly, whereas soluble protein and pectin content decreased appreciably. Therefore, the use of I‐PG provided an effective and feasible method for improving quality of the pumpkin–hawthorn juice. Practical applications In order to overcome the drawbacks of using free pectinase and glucoamylase, an effective method for the co‐immobilization of these two enzymes onto sodium alginate/graphene oxide beads was developed. The co‐immobilized pectinase/glucoamylase developed in this study could be applied in the clarification of juice rich in pectin and starch.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

et al. 2018

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“…The prepared nanobiocatalyst was characterized by FT-IR, SEM and XRD. Finally, the clarification of apple, grapes and pineapple juices using magnetic tri-enzyme showed 41%, 46% and 53% respective reduction in turbidity till 150min treatment 93 .…”

Section: Introductionmentioning

confidence: 92%

Emerging Applications of Fermented Fruit Enzyme Beverages as Nutraceutical, Functional Food, and Designer Food Products: A Review

Kumar¹,

Saini²,

Meenakshi³

et al. 2018

J. Pharm. Sci. Innov.

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In the past, the beneficial effects of fermented fruits were unknown, and so people primarily used fermentation to preserve fruits, enhance shelf life, and improve flavor. Fermentation of fruits has been adopted over many generations, primarily due to their commercial significance. Edible tropical fruits such as, cashew apple, mangoes, papaya, pineapple, litchi, guava, bael, banana, pomegranate, jamun and palm etc. with high export potential have their origin in the tropics and require rather suitable climatic conditions; and can not tolerate environmental stress. Most of the tropical fruits are important sources of antioxidants, vitamins and minerals and form a very healthy part of a diet. An effective utilisation of inferior grade and over-ripe fruits and processing them into fermented beverages has been revealed as a new and promising alternative to generate extra revenues whilst conducting a sustainable exploitation of wastes. In addition, microorganisms contributing to the fermentation process have recently been associated with many health benefits, and so these microorganisms have become another focus of attention. This paper reviews the production techniques and beneficial health effects of different fermented fruits. Scientific advances in the emerging area of functional beverages; as they provide a health benefit beyond the basic nutritional functions also reported in this paper.

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“…However, previous studies using a complex of hydrolytic enzymes immobilized on magnetic particles have reported activity drops to 20% after the second reuse cycle [16,28]. The reduction of the residual activity of the enzymes during the recycling test could be due to product inhibition, mechanical damage, or deactivation of the enzyme [31,32]. This effect was attributed to leakage of the enzyme from the support, due to the lixiviation of non-covalently bound enzyme molecules adsorbed on the support during the first reaction cycle.…”

Section: Reuse Capacity Of Fe 3 O 4 @Chitosan@enzymesmentioning

confidence: 98%

Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

et al. 2019

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Enzyme immobilization on different supports has emerged as an efficient and cost-effective tool to improve their stability and reuse capacity. This work aimed to produce a stable immobilized multienzymatic system of xylanase and filter paper-ase (FPase) onto magnetic chitosan using genipin as a cross-linking agent and to evaluate its biochemical properties and reuse capacity. A mixture of chitosan magnetic nanoparticles, xylanase, and FPase was covalently bonded using genipin. Immobilization yield and efficiency were quantified. The activity of free and immobilized enzymes was quantified at different values of pH, temperature, substrate concentration (Km and Vmax), and reuse cycles. The immobilization yield, immobilization efficiency, and activity recovery were 145.3% ± 3.06%, 14.8% ± 0.81%, and 21.5% ± 0.72%, respectively, measured as the total hydrolytic activity. Immobilization confers resistance to acidic/basic conditions and thermal stability compared to the free form. Immobilization improved 3.5-fold and 78-fold the catalytic efficiency (Kcat/Km) of the xylanase and filter paper-ase activities, while immobilized xylanase and FPase could be reused for 34 min and 43 min, respectively. Cross-linking significantly improved the biochemical properties of immobilized enzymes, combined with their simplicity of reuse due to the paramagnetic property of the support. Multienzyme immobilization technology is an important issue for industrial applications.

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A magnetic tri-enzyme nanobiocatalyst for fruit juice clarification

Cited by 116 publications

References 37 publications

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

Co-immobilization of pectinase and glucoamylase onto sodium aliginate/graphene oxide composite beads and its application in the preparation of pumpkin-hawthorn juice

Emerging Applications of Fermented Fruit Enzyme Beverages as Nutraceutical, Functional Food, and Designer Food Products: A Review

Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

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