Extraction and Purification of Lipoxygenase from Soybean Using Aqueous Two-Phase System

Lakshmi, M. C.; Madhusudhan, M. C.; Raghavarao, K.S.M.S.

doi:10.1007/s11947-009-0278-8

Cited by 19 publications

(5 citation statements)

References 24 publications

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“…As a result, the biomolecules will selectively partition to the bottom phase. Similar results were observed by Nandini and Rastogi [26], Priyanka et al [29], and Lakshmi et al [30]. The specific activity of the top and bottom phases and yield and purification factor for the bottom phase in the systems with different PEGs (MW 1000, 2000, 4000, and 6000) are shown in Table 2.…”

Section: Effect Of Peg Molecular Weightsupporting

confidence: 86%

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Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

Vinayagam

Murty

2015

Bioresour. Bioprocess.

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Background: A major challenge in downstream processing is the separation and purification of a target biomolecule from the fermentation broth which is a cocktail of various biomolecules as impurities. Aqueous two phase system (ATPS) can address this issue to a great extent so that the separation and partial purification of a target biomolecule can be integrated into a single step. In the food industry, starch production is carried out using thermostable glucoamylase. Humicola grisea serves as an attractive source for extracellular production of glucoamylase. Results: In the present investigation, the possibility of using polyethylene glycol (PEG)/salt-based ATPS for the partitioning of glucoamylase from H. grisea was investigated for the first time. Experiments were conducted based on one variable at a time approach in which independent parameters like PEG molecular weight, type of phase-forming salt, tie line length, phase volume ratio, and neutral salt concentration were optimized. It has been found that the PEG 4000/potassium phosphate system was suitable for the extraction of glucoamylase from the fermentation broth. From the results, it was observed that, at a phase composition of 22 % w/w PEG 4000 and 12 % w/w phosphate in the presence of 2 % w/w NaCl and at pH 8, glucoamylase was partitioned into the salt-rich phase with a maximum yield of 85.81 %.

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Section: Effect Of Peg Molecular Weightsupporting

confidence: 86%

“…The purification factor increased and reached a maximum value of 1.72 at TLL of 30.62 %. A decrease in the purification factor value was observed for further increase in TLL, and this may be due to the high salt concentration at the bottom phase which affects the solubility of glucoamylase [30].…”

Section: Effect Of Tllmentioning

confidence: 98%

Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

Vinayagam

Murty

2015

Bioresour. Bioprocess.

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“…Similar interrelationship was also found by [41] by using PEG-phosphate systems with PEG molecular weight 600 to 20,000. Similar results were observed by [42][43][44][45].…”

Section: Effect Of Peg Molecular Weight On Partitioning Of Proteasesupporting

confidence: 89%

Utilization of Integrative Technique for Partial Recovery of Proteases from Soil Microbes

Nawab

Aasim

Saddique

et al. 2018

Period. Polytech. Chem. Eng.

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Aqueous two-phase system (ATPS) is an efficient, cost effective, fast, simple and ecofriendly method for the recovery of biomolecules. In the present study, an ATPS composed of polyethylene glycol and ammonium sulphate (NH4)2SO4 was used for the partial purification of proteases from microbial source. The effects of different parameters such as molecular weight of PEG (4000, 6000 and 10000), concentration of PEG (15, 17.5 and 20 %) and concentration of (NH4)2SO4 (7.5, 8.3, 9.1 and 9.9 %) on the partitioning behavior of proteases at room temperature were investigated. Generally, increasing the concentration of PEG and (NH4)2SO4 moved the protease to the top i.e., polymer-rich phase. Increasing the molecular weight of PEG from 4000 to 10000 the partition coefficient decreased subsequently. The highest partition coefficient i.e., 3.32 and maximum activity i.e., 16.06 soxhlet unit was found in an optimum system composed of 20 % PEG 4000 and 9.9 % (NH4)2SO4.

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“…Aqueous extraction of soybean flour yields a complex mixture of protein, peptides, carbohydrates, oligosaccharides, pigments, and other low‐molecular‐mass compounds (Lakshmi and others ). Purification of LOX from this complex mixture is further complicated by the presence of multiple isoforms with similar molecular mass and p I values (Axelrod ; Diel and Stan ; Faubion and Hoseney ; Shiiba and others ; Chedea and Jisaka ).…”

Section: Molecular Enzymology Of Loxmentioning

confidence: 99%

Lipoxygenases: From Isolation to Application

Hayward

Cilliers

Swart

2016

Comp Rev Food Sci Food Safe

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The positive effect of lipoxygenase, added as an enzyme-active soy flour, during the production of white bread is well established. In addition to increasing the mixing tolerance and overall dough rheology, lipoxygenase is also an effective bleaching agent. It is known that these effects are mediated by enzyme-coupled cooxidation of gluten proteins and carotenoids. However, the mechanism whereby these effects are achieved is not yet fully understood. In order to gain a better understanding into the reactions governing the beneficial effects of lipoxygenases in bread dough, an in-depth knowledge of the lipoxygenase catalytic mechanism is required. Until now no single review combining the molecular enzymology of lipoxygenase enzymes and their application in the baking industry has been presented. This review, therefore, focuses on the extraction and molecular characterization of lipoxygenases in addition to the work done on the application of lipoxygenases in the baking industry.

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Extraction and Purification of Lipoxygenase from Soybean Using Aqueous Two-Phase System

Cited by 19 publications

References 24 publications

Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

Partitioning of thermostable glucoamylase in polyethyleneglycol/salt aqueous two-phase system

Utilization of Integrative Technique for Partial Recovery of Proteases from Soil Microbes

Lipoxygenases: From Isolation to Application

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