Enzyme Production

Illanes, Andrés

doi:10.1007/978-1-4020-8361-7_2

Cited by 52 publications

(83 citation statements)

References 350 publications

(287 reference statements)

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“…The marketable bromelain is mostly extracted from the stem of pineapple through centrifugation, ultrafiltration, lyophilization (Corzo et al 2011) and two-step Fast Protein Liquid Chromatography (FPLC) (Harrach et al 1998). Once extracted, the crude mixture containing required enzyme is then exposed to numerous purification stages to eradicate impurities that may interfere with bromelain to hinder its application and reduce the specific activity of the enzyme (Illanes 2008). Product purity is the key factor which may constitute a large proportion of the total enzyme production cost (Lightfoot 1990).…”

Section: Extraction and Purification Methodsmentioning

confidence: 99%

Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Manzoor

Nawaz

Mukhtar

et al. 2016

Braz. arch. biol. technol.

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Section: Extraction and Purification Methodsmentioning

confidence: 99%

Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Manzoor

Nawaz

Mukhtar

et al. 2016

Braz. arch. biol. technol.

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“…A high value for E ia is characteristic for thermostable enzymes, while low values point to thermosensitive enzymes. For most enzymes, the activation energy of deactivation can be found within 84 -837 kJ/mol [46]. The E ia was 84.45 kJ/mol indicating that the studied rDyP is in the higher thermosensitive zone [46].…”

Section: Temperature Effect On Enzymatic Activitymentioning

confidence: 91%

Novel DyP from the basidiomycete Pleurotus sapidus: substrate screening and kinetics

Avram¹,

Sengupta²,

Pfromm³

et al. 2018

Biocatalysis

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A novel Dye-decolorizing peroxidase from the basidiomycete Pleurotus sapidus was screened for dyedecolorizing peroxidase activity with 2,2‘-azino-bis(3- ethylbenzothiazoline-6-sulfonic acid), Remazol Brilliant Blue R and Guaiacol. Additionally, the catalytic efficiency on degrading β-carotene into volatile products, and the catalyst storage stability with three different additives were also studied. The apparent inhibition constant (KS) was 51.7 μM. Optimal reaction rates (Vmax) and affinity constants (Km) towards the reducing substrates were obtained using Michaelis-Menten kinetic theory. The trend in the calculated Km’s was found to be 7.0 mM > 0.524 mM > 0.051 mM for Guaiacol, 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and Remazol Brilliant Blue R. The storage stability of the catalyst was evaluated with 7.0% w/v PEG400, 7.0% w/v PEG1450 and 0.1% w/v Tween®80 at 5°C over a period of 45 days. The study revealed the longest activity conservation with PEG1450, where rDyP had lost 30% of initial activity. The enzyme solution presented similar pH and temperature dependence to known fungal dye-decolorizing peroxidases with most prolific enzymatic activities registered at pH 4.0 and temperatures below 30°C. An interesting property of the catalyst was oxidation observed in the absence of hydrogen peroxide.

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“…The temperature will have a major impact not only on the enzyme activity but also on the stability of the enzyme. An increase in temperature resulted in an increase in the rate of catalytic reactions, while it also increased the rate of enzyme inactivation [21]. …”

Section: The Effect Of Initial Substrate Concentration On Degree Of Hmentioning

confidence: 99%

Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

Yanti¹,

Hastuti²,

Sulistyo³

et al. 2016

AIP Conference Proceedings

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Abstract. The seedcake of nyamplung seeds still contains high protein. Recent studies show that protein hydrolysate has many useful effects, such as an antioxidant. The protein was isolated by the isoelectric precipitation method, further on hydrolysed into short chain peptides. The chemical composition of seedcake and the protein content of extract were analysed. The hydrolysis of the extract was carried out in a various condition such as substrate concentration, pH, and temperature for a different length of hydrolysis and the degree of hydrolysis was determine by TNBS method. The protein isolation process performed on the defatted seedcake produced 52.84 ± 0.07% of protein extract with a brownish colour. The degree of hydrolysis (DH) was increased by increasing the length of hydrolysis and showed the optimum DH with 6.15mg/mL substrate concentration. The increase of temperature also increased the DH, however at 70°C with 240 min time reaction, the DH tended to decrease. The pH of reaction between papain showed the similar DH among various pH of the reaction, with pH 7 showed the stable increasing DH till 240 min of reaction. The antioxidant activity showed an increase to 90% of inhibition by the addition of the hydrolysate to the system until 1300 ppm. However, the addition of more than 1300 ppm showed a reduction activity

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Enzyme Production

Cited by 52 publications

References 350 publications

Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Bromelain: Methods of Extraction, Purification and Therapeutic Applications

Novel DyP from the basidiomycete Pleurotus sapidus: substrate screening and kinetics

Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

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