Three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

Gagaoua, Mohammed; Hoggas, Naouel; Hafid, Kahina

doi:10.1016/j.ijbiomac.2014.10.069

Cited by 62 publications

(28 citation statements)

References 56 publications

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“… This paper describes data related to a research article titled “Three Phase Partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes” (Gagaoua et al, 2015) [1] . Zingibain (EC 3.4.22.67), is a coagulant cysteine protease and a meat tenderizer agent that have been reported to produce satisfactory final products in dairy and meat technology, respectively.…”

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Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

2016

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This paper describes data related to a research article titled “Three Phase Partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes” (Gagaoua et al., 2015) [1]. Zingibain (EC 3.4.22.67), is a coagulant cysteine protease and a meat tenderizer agent that have been reported to produce satisfactory final products in dairy and meat technology, respectively. Zingibains were exclusively purified using chromatographic techniques with very low yield purification. This paper includes data of the effect of temperature, usual salts and organic solvents on the efficiency of the three phase partitioning (TPP) system. Also it includes data of the kinetic activity characterization of the purified zingibain using TPP purification approach.

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Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

2016

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“…The plants studied initially had all micro-constituent less than 5 kDA removed to evaluate the ability of the plant to cleave milk proteins; this was done mostly because plant proteases are generally larger (Gagaoua et al, 2015). Apart from proteolytic coagulation, milk is known to coagulate as a result of exposure to low pH levels.…”

Section: Discussionmentioning

confidence: 99%

Tropical Fruits of Mango and Noni Having Dual Effects of Coagulating Milk and Enriching the Curds With Micro-Constituents of Medicinal Potential

Vejayan

Munir

Lian

et al. 2019

MJS

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Plants are capable of coagulating milk efficiently and enriching the curd with medicinal potentials, which can result in an ideal functional dairy food. Such efforts were attempted within this study with two fruit bearing plants, Mango (Mangifera indica) and Noni (Morinda citrifolia). The extracts of the two plants were separated to their enzymatic fractions and investigated for their coagulating time in comparison to rennet enzyme of Mucor miehei. The biological activities of the curd formed by the extracts were evaluated to determine the antioxidant and antidiabetic activities. The coagulation of milk by M. indica seed fraction, M. citrifolia fruit fraction and the rennet (15%, 15%, and 5% (w/v), respectively) resulted in coagulation times of 10.8 ± 0.36 s, 40.73 ± 1.91 s and 198.2 ± 1.01 s, respectively. Curd by aqueous extract of M. indica seeds resulted in the most favourable values: IC50 = 3.266 ± 0.353 μg/mL (2,2-diphenyl-1picylhydrazyl, DPPH), 147.329 ± 1.890 mg GAE/g (Ferric Reducing Antioxidant Power, FRAP), IC50 = 17.87 ± 0.415 μg/mL (α-glucosidase inhibition) and IC50 = 41.87 ± 0.585 μg/mL (α-amylase inhibition). Hence, M. indica seed and M. citrifolia fruit extracts were tested, and both plant extracts, together with curd-fortification, exhibited useful biological activities. ABSTRAK Tumbuhan herba mampu mengentalkan susu segar kepada dadih dan seterusnya memperkayakannya dengan aktiviti biologi berguna bagi penghasilan makanan tenusu berfungsi. Usaha-usaha seperti ini telah dicuba dalam kajian ini dengan dua buah tanaman berbuah; Morinda citrifolia dan Mangifera indica. Ekstrak kedua-dua tumbuhan telah dipisahkan kepada pecahan enzimatik mereka dan diselidiki kebolehan untuk pengentalan susu berbanding dengan enzim rennet daripada sumber Mucor miehei. Aktiviti biologi dadih yang dibentuk oleh ekstrak telah dinilai untuk menentukan aktiviti antioksidan dan antidiabetik. Kebolehan pengentalan susu oleh fraksi kromatografi daripada M. indica, M. citrifolia dan rennet (15%, 15% dan 5% (w / v) masing-masing menghasilkan masa pengentalan singkat seperti berikut, 10.8 ± 0.36 s, 40.73 ± 1.91 s dan 198.2 ± 1.01 s, masing-masing. Dadih diperkuat dengan ekstrak berair biji M. indica menghasilkan nilai yang paling baik: IC50 = 3.266 ± 0.353 μg / mL (2,2-diphenyl-1-picylhydrazyl, DPPH), 147.329 ± 1.890 mg GAE / g (FRAP), IC50 = 17.87 ± 0.415 μg / mL (rencatan αglucosidase) dan IC50 = 41.87 ± 0.585 μg / mL (rencatan α-amylase). Kesimpulannya, biji M. indica dan ekstrak buah M. citrifolia diuji, dan kedua-dua ekstrak tumbuhan, selain kebolehan untuk mengental susu juga mempamerkan aktiviti biologi yang berguna.

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“…The culture supernatant containing secreted xylanases was concentrated using Sartorius membranes (with 10-kDa cutoff membrane; Millipore) after a centrifugation at 10,000 rpm for 10 min. Then, TPP experiments were carried out following the recommendations of Gagaoua et al (2015). The enzyme exclusively recovered in the interfacial phase was gently separated from the other phases and dissolved in 50 mM Tris–HCl buffer (pH 8.5) and dialyzed overnight at 4–5 °C and used for enzyme characterization.…”

Section: Methodsmentioning

confidence: 99%

“…Also, preliminary investigation using three phase partitioning (TPP) system (Gagaoua et al 2014; Gagaoua and Hafid 2016) for xylanase purification was performed. In TPP process, firstly an inorganic salt (generally ammonium sulfate) is added to the crude extract containing proteins then mixted with tert -butanol in an appropriate amount (Gagaoua et al 2015, 2016, 2017). When t -butanol is added in the presence of ammonium sulfate, it pushes the protein out of the solution.…”

Section: Introductionmentioning

confidence: 99%

Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract of Bacillus oceanisediminis strain SJ3

Boucherba

Gagaoua

Bouanane‐Darenfed

et al. 2017

Bioresour. Bioprocess.

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The present study investigates the production and partial biochemical characterization of an extracellular thermostable xylanase from the Bacillus oceanisediminis strain SJ3 newly recovered from Algerian soil using three phase partitioning (TPP). The maximum xylanase activity recorded after 2 days of incubation at 37 °C was 20.24 U/ml in the presence of oat spelt xylan. The results indicated that the enzyme recovered in the middle phase of TPP system using the optimum parameters were determined as 50% ammonium sulfate saturation with 1.0:1.5 ratio of crude extract: t-butanol at pH and temperature of 8.0 and 10 °C, respectively. The xylanase was recovered with 3.48 purification fold and 107% activity recovery. The enzyme was optimally active at pH 7.0 and was stable over a broad pH range of 5.0–10. The optimum temperature for xylanase activity was 55 °C and the half-life time at this temperature was of 6 h. At this time point the enzyme retained 50% of its activity after incubation for 2 h at 95 °C. The crude enzyme resist to sodium dodecyl sulfate and β-mercaptoethanol, while all the tested ions do not affect the activity of the enzyme. The recovered enzyme is, at least, stable in tested organic solvents except in propanol where a reduction of 46.5% was observed. Further, the stability of the xylanase was higher in hydrophobic solvents where a maximum stability was observed with cyclohexane. These properties make this enzyme to be highly thermostable and may be suggested as a potential candidate for application in some industrial processes. To the best of our knowledge, this is the first report of xylanase activity and recoverey using three phase partitioning from B. oceanisediminis.

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Three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

Cited by 62 publications

References 56 publications

Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes

Tropical Fruits of Mango and Noni Having Dual Effects of Coagulating Milk and Enriching the Curds With Micro-Constituents of Medicinal Potential

Biochemical properties of a new thermo- and solvent-stable xylanase recovered using three phase partitioning from the extract of Bacillus oceanisediminis strain SJ3

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