Comparative characterization of monophenolase and diphenolase activities from a wild edible mushroom (Macrolepiota mastoidea)

Kolcuoğlu, Yakup; Çolak, Ahmėt; Sesli, Ertuğrul; Yildirim, Melike; Saglam, Nagihan

doi:10.1016/j.foodchem.2006.02.035

Cited by 22 publications

(14 citation statements)

References 44 publications

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“…Interestingly, we found a very strong correlation (r = 0.85; P = 0.07) between copper content of fruit and PPO activity (Table 6). According to Aydemir (2004), Cu ++ and Fe +++ ions at 1 mM caused the activation of PPO, but at 10 mM concentration, both Cu ++ and Fe +++ ions acted as poor inhibitors of PPO, whereas, Colak et al (2007) and Kolcuoglu et al (2007) have recently found that Cu ++ at 1 mM concentration was sufficient to inhibit PPO activity. As well, the reported literature on the effects of different metal ions on the PPO activity is conflicting.…”

Section: Resultsmentioning

confidence: 99%

Biochemical characterization of enzymatic browning in selected apple genotypes

Joshi¹,

Rupasinghe

Pitts³

et al. 2007

Can. J. Plant Sci.

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S. 2007. Biochemical characterization of enzymatic browning in selected apple genotypes. Can. J. Plant Sci. 87: 1067-1074. Enzymatic browning in apples (Malus × domestica Borkh.) caused by polyphenol oxidases (PPO) is the major factor responsible for the deterioration of quality in processed apple products such as juice, fresh-cut slices, and chips. Selected apple genotypes with a range of low post-cut enzymatic browning were investigated to understand the biochemical mechanisms leading to enzymatic browning. Post-cut enzymatic browning, polyphenolic profiles using LC-MS/MS, PPO activity, vitamin C, total antioxidant capacity using the Ferric Reducing Antioxidant Power (FRAP) and the Oxygen Radical Absorbance Capacity (ORAC), and elemental composition were determined in two recently released cultivars [Eden TM (also known as SJCA38R6A74) and SuperMac], and one new advanced line (SJCA16) and compared with two commercial cultivars (Empire and Cortland). Eden TM exhibited the least post-cut enzymatic browning as estimated by Whiteness Index. SJCA16 possessed a characteristic yellowish flesh color. Whiteness Index (WI) values were inversely related to chlorogenic acid, catechin and epicatechin contents present in apple slices. Vitamin C content showed a strong positive correlation with WI. Among the mineral elements, the content of copper had a strong positive correlation with PPO activity.

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Section: Resultsmentioning

confidence: 99%

Biochemical characterization of enzymatic browning in selected apple genotypes

Joshi¹,

Rupasinghe

Pitts³

et al. 2007

Can. J. Plant Sci.

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“…Antioxidant activity in acidified by 0.5% HCl methanol extracts (40 mg sample/1 ml extract) was assayed for scavenging capacity of the DPPH radical (Pekkarinen et al, 1999) and ABTS cation radical (Re et al, 1999). Total polyphenoloxidases activity (PPO) was determined according to Cano et al (1997), peroxidase (PER) and catalase (CAT) activity according to Bergmeyer (1974), monophenolase (MON) and diphenolase (DIP) according to Kolcuoglu et al (2007). Analyses were carried out in four replications for each sample.…”

Section: Methodsmentioning

confidence: 99%

“…The antioxidant enzymes scavenged O 2 -and H 2 O 2 , which peroxidation and accelerated cell senescence. According toKolcuoglu et al (2007), monophenolase in mushrooms can be inhibited by thiourea and ascorbic acid, and diphenolase by sodium metabisulphite and ascorbic acid.The activity of catalase (CAT), total polyphenol oxidase (PPO), monophenolase (MON) and diphenolase (DIP) in fresh A. bisporus mushrooms was determined. In the case of peroxidase activity, zero or trace levels were detected in both fresh and frozen mushrooms (Tab.…”

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confidence: 99%

Use of onion extract to prevent enzymatic browning of frozen Agaricus bisporus mushrooms

Bernaś

Jaworska

2015

International Journal of Refrigeration

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“…For example, for commercial mushroom PPO, the loss of monophenolase activity was observed at pH 3.0, 4.0 and 5.0, while the enzyme is very stable at pH 6.0 [18]. The same phenomenon was observed at pH 3.0 for the monophenolase activity of a wild edible mushroom (Macrolepiota mastoidea), while the enzyme showed highest stability at pH 4.0 [38]. The loss of labile monophenolase activity was also frequently observed during purification of PPO by different workers [2,39,40].…”

Section: Ph Stabilitymentioning

confidence: 65%

Partial purification and kinetic characterization of mushroom stem polyphenoloxidase and determination of its storage stability in different lyophilized forms

Şimşek¹,

Yemenicioğlu²

2007

Process Biochemistry

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Monophenolase (1011 AE 626 U/g AP) and diphenolase activities (5163 AE 3059 U/g AP) of PPO in acetone powders (APs) of different mushroom stems varied considerably. However, the limited variation of average dipenolase (L-DOPA) to monophenolase (L-tyrosine) activity ratio (5.4 AE 0.7) in crude extracts showed the homogeneity of PPO from different mushroom stems. The change in extraction material or partial purification method (ammonium sulfate or acetone precipitation) did not affect the temperature stability, temperature and pH dependency and K m of monophenolase activity considerably. However, some changes were observed in pH stability and substrate specificity of PPO in different parties of mushroom stems. The most important aspects of mushroom stem PPO are its lower diphenolase to monophenolase activity ratio than mushroom cap PPO, low temperature dependency of activity between 25 and 40 8C (E a = 30 kJ/mol), broad optimum pH between 6 and 8, but lack of activity pH 5, and ability to use phloridzin as substrate. The mushroom stem PPOs partially purified and lyophilized by using sucrose, dextran or alginate showed moderate to high stability at À18 8C for 6-6.5 months. Thus, the mushroom stems obtained as a waste material during mushroom processing may be used as a more homogenous source than whole mushrooms to obtain PPO used for different industrial, clinical or research purposes. #

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Comparative characterization of monophenolase and diphenolase activities from a wild edible mushroom (Macrolepiota mastoidea)

Cited by 22 publications

References 44 publications

Biochemical characterization of enzymatic browning in selected apple genotypes

Biochemical characterization of enzymatic browning in selected apple genotypes

Use of onion extract to prevent enzymatic browning of frozen Agaricus bisporus mushrooms

Partial purification and kinetic characterization of mushroom stem polyphenoloxidase and determination of its storage stability in different lyophilized forms

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