Investigation of biocatalytic properties of soybean seed hull peroxidase

Geng, Zuohong; Rao, K. Jagannadha; Bassi, Amarjeet; Gijzen, Mark; Krishnamoorthy, Nupura

doi:10.1016/s0920-5861(00)00527-7

Cited by 36 publications

(23 citation statements)

References 8 publications

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“…This outcome contrasts previous results, which indicated that quercetin oxidation, the physiological substrate of the enzyme, by a crude onion peroxidase extract was favoured at pH 8 (Takahama and Hirota 2000). Peroxidases from other plant residual sources that have been used in studies pertaining to phenol removal, such as HRP (Tong et al 1997), SBP (Wright and Nicell 1999;Geng et al 2001), TNP (Duarte-Vázquez et al 2002) and bitter gourd peroxidase-BGP (Akhtar and Husain 2006), showed optimal pH around 7, 6, 7 and 6, respectively. In these cases too it was seen that pH optimum may differ significantly with different substrates.…”

Section: The Effect Of H 2 O 2 Ph and Temperaturecontrasting

confidence: 97%

“…The temperature at which optimum activity was attained (30°C) is close to that found for BGP and HRP (Akhtar et al 2005;Bódalo et al 2006;Yamada et al 2007), which lied between 30°C and 40°C, and somewhat lower than TMP that showed an optimum between 40°C and 50°C (González et al 2006). By contrast, SBP has been reported to be much more active at 22 than at 4°C (Kennedy et al 2002), while other studies demonstrated that SBP is even more active at 80°C than at 20°C (Geng et al 2001).…”

Section: The Effect Of H 2 O 2 Ph and Temperaturesupporting

confidence: 71%

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Biocatalytic properties of a peroxidase-active cell-free extract from onion solid wastes: caffeic acid oxidation

et al. 2008

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The exploitation of food residual sources consists of a major factor in reducing the polluting load of food industry wastes and developing novel added-value products. Plant food residues including trimmings and peels might contain a range of enzymes capable of transforming bio-organic molecules with potential phytotoxicity, including hydrolases, peroxidases and polyphenoloxidases. Although the use of bacterial and fungal enzymes has gained interest in studies pertaining to bioremediation applications, plant enzymes have been given less attention or even disregarded. In this view, this study aimed at the investigating the use of a crude peroxidase preparation from onion solid by-products for oxidising caffeic acid, a widespread o-diphenol, whose various derivatives may occur in food industry wastes, such as olive mill waste waters. Increased enzyme activity was observed at a pH value of 5, but considerable activity was also retained for pH up to 7. Favourable temperatures for increased activity varied between 20 degrees C and 40 degrees C, 30 degrees C being the optimal. Liquid chromatography-mass spectrometry analysis of a homogenate/H(2)O(2)-treated caffeic acid solution revealed the existence of a tetramer as major oxidation product. Based on the data generated, a putative pathway for the formation of the peroxidase-mediated caffeic acid tetramer was proposed.

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Section: The Effect Of H 2 O 2 Ph and Temperaturecontrasting

confidence: 97%

Section: The Effect Of H 2 O 2 Ph and Temperaturesupporting

confidence: 71%

Biocatalytic properties of a peroxidase-active cell-free extract from onion solid wastes: caffeic acid oxidation

et al. 2008

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“…Thus, among these solvents, peroxidase exhibited maximum tolerance towards methanol that could be suggested as a better organic solvent followed by ethanol and isopropanol. Similar to our observation soybean seed hull peroxidase has been reported to retain considerable activity in the presence of methanol and ethanol [24]. Furthermore, immobilized Momordica peroxidase has been reported to retain 43% activity in presence of propanol (30%) [36].…”

Section: Effects Of Organic Solvents On Purified Peroxidasesupporting

confidence: 90%

“…The importance of peroxidases in polymer chemistry is based on their ability to oxidize a variety of phenolic molecules which provide ideal sites for cross-linking leading to polymerization reactions. The grafting applications become an important industrial application of peroxidases [24].…”

Section: Introductionmentioning

confidence: 99%

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

Veda¹,

ey²,

Bhagat³

et al. 2016

Biochem Anal Biochem

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Peroxidases have ability to catalyze redox reaction of a wide range of phenolic as well as non-phenolic compounds and exhibited various physiological roles in plant life cycle. From the point of view of industrial applications of peroxidases, the isolation and characterization of peroxidases offering resistance to higher pH and temperature, salts, organic solvents is highly desirable. In this direction, a partial cDNA clone of peroxidase from lemon was isolated and characterized. The peroxidase was found to be defense associated as evident by the higher expression in diseased condition than that of healthy one at both the transcript and enzymatic activity levels. This defense related peroxidase from lemon leaves was purified to homogeneity using quick two step processes of heat treatment and affinity chromatography. The native peroxidase was found to be a heterotrimer of 200 kDa, consisting of two subunits each of 66 kDa while, one subunit of 70 kDa. The purified peroxidase was found to be stable towards heat (retained 92% activity at 80°C for 1 h) and organic solvents, namely ethanol, methanol and isopropanol (retained 30-50% activity in the presence of 50% (v/v) of these solvents for 1 h). Purified peroxidase also exhibited tolerance to heavy metal ions such as Cd 2+ , Ni 2+ and Cs 2+ . The purified lemon peroxidase was found to efficiently oxidize the industrial dyes in the order of aniline blue>methyl orange> indigo carmine >trypan blue > crystal violet, such that 40-54% dye decolorization was observed within 4 h. Thus, the properties exhibited by purified lemon peroxidase make it a promising candidate enzyme for industrial exploitation.

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“…Most of these investigations mainly deal with the use of soluble SBP [21][22][23][24][25], although some authors use the seedhulls directly [26,27] as catalyst or the peroxidase entrapped within hybrid (silica solgel/alginate) particles [28].…”

Section: Introductionmentioning

confidence: 99%

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

Bódalo

Bastida

Máximo

et al. 2008

Bioprocess Biosyst Eng

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Horseradish peroxidase (HRP) and soybean peroxidase (SBP) were covalently immobilized onto aldehyde glass through their amine groups. The activity yield and the protein content for the immobilized SBP were higher than for the immobilized HRP. When free and immobilized peroxidases were tested for their ability to remove 4-chlorophenol from aqueous solutions, the removal percentages were higher with immobilized HRP than with free HRP, whereas immobilized SBP needs more enzyme to reach the same conversion than free enzyme. In the present paper the two immobilized derivatives are compared. It was found that at an immobilized enzyme concentration in the reactor of 15 mg l(-1), SBP removed 5% more of 4-chlorophenol than HRP, and that a shorter treatment was necessary. Since immobilized SBP was less susceptible to inactivation than HRP and provided higher 4-chlorophenol elimination, this derivative was chosen for further inactivation studies. The protective effect of the immobilization against the enzyme inactivation by hydrogen peroxide was demonstrated.

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Investigation of biocatalytic properties of soybean seed hull peroxidase

Cited by 36 publications

References 8 publications

Biocatalytic properties of a peroxidase-active cell-free extract from onion solid wastes: caffeic acid oxidation

Biocatalytic properties of a peroxidase-active cell-free extract from onion solid wastes: caffeic acid oxidation

A Defense Associated Peroxidase from Lemon Having Dye Decolorizing Ability and Offering Resistance to Heat, Heavy Metals and Organic Solvents

A comparative study of free and immobilized soybean and horseradish peroxidases for 4-chlorophenol removal: protective effects of immobilization

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