High-yield production of a low-temperature-active polygalacturonase for papaya juice clarification

Tu, Tao; Meng, Kun; Bai, Yingguo; Shi, Pengjun; Luo, Huiying; Wang, Yaru; Yang, Peilong; Zhang, Yuhong; Zhang, Wei; Yao, Bin

doi:10.1016/j.foodchem.2013.05.132

Cited by 71 publications

(84 citation statements)

References 29 publications

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“…The degradation was mainly caused by native oxidative enzymes which could be prevented by pretreatment such as HB or SO 2 (Rossi et al, 2003, Lee et al, 2002. To improve the juice yield, enzymatic clarification is thus a requiring step which applies pectinase to lower the viscosity, turbidity and water binding capacity of pectin for easier extraction of components (Tu et al, 2013). Phytochemicals have been studied during juice clarification (Spanos et al, 1992;Skrede et al, 2000, Rinaldi et al, 2013, but few investigations on plum juice (Chang et al, 1994).…”

Section: Abbreviations Usedmentioning

confidence: 99%

Effect of Juicing On Nutrition Qualities of “Sanhua” Plum (Prunus Salicina Lindl.) Juice from 4 Cultivars

Chao

Duan

Liu

et al. 2014

FSTR

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"Sanhua" plums of 4 cultivars were processed into juice. Pretreatment including heat blanching (HB), microwave blanching (MB) and SO 2 were studied on the inactivation of polyphenoloxidase (PPO), peroxidase (POD) and nutrition qualities. Enzymatic clarification, pasteurization and UHT were also investigated on nutrition qualities. Results showed that PPO and POD could be almost inactivated by HB (95℃

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Section: Abbreviations Usedmentioning

confidence: 99%

Effect of Juicing On Nutrition Qualities of “Sanhua” Plum (Prunus Salicina Lindl.) Juice from 4 Cultivars

Chao

Duan

Liu

et al. 2014

FSTR

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“…solo 8 polygalacturonase (3.62 UI/mg protein) obtained was less than polygalacturonase of Achaetomium sp. Xz8 (28.122 UI/mg protein) (Tu et al, 2013) and polygalacturonase of Aspergillus niger MTCC 3323 (54.3 UI/mg protein) (Arotupin et al, 2012). Otherwise, specific activity of papaya pericarp cv.…”

Section: Resultsmentioning

confidence: 99%

“…KSM-P 410 (pH 7) (Jayani et al, 2005). Polygalacturonase from Carica papaya pericarp could be favorable for the treatment in acid medium such as papaya juice (pH 5.6) (Tu et al, 2013). Whereas maximum pectin lyase activity at pH 8.0 confirms the alkalophilic nature of pectin lyase partially purified.…”

Section: Characterization Of Polygalacturonase and Pectin Lyasementioning

confidence: 94%

“…degradation of pectic substances is essential (Favela-Torres et al, 2005). Polygalacturonase and pectin lyase have a great commercial significance in industrial application (Kashyap et al, 2001;Khan et al, 2013;Tu et al, 2013;Kumar and Suneetha, 2014). Whereas most industrial production of pectinases is limited to some species of bacteria, yeast (Gummadi and Panda, 2003;Jayani et al, 2005;Combo et al, 2012).…”

Section: Issn: 2319-7706 Volume 6 Number 6 (2017) Pp 2729-2739mentioning

confidence: 99%

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Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

Didier¹,

Hubert²,

Parfait³

et al. 2017

Int.J.Curr.Microbiol.App.Sci

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“…PG8fn from Achaetomium sp. strain Xz8 is distinguished by its high specific activity (28,000 Ϯ 293 U/mg) and broad ranges of pH adaptation and stability (pH 3.0 to 8.0) (29). However, its thermal properties are poor: it retains thermostability only at 45°C or below.…”

Section: Improvement In Thermostability Of An Achaetomium Sp Strain mentioning

confidence: 99%

Improvement in Thermostability of an Achaetomium sp. Strain Xz8 Endopolygalacturonase via the Optimization of Charge-Charge Interactions

Luo

Meng

et al. 2015

Appl Environ Microbiol

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bImproving enzyme thermostability is of importance for widening the spectrum of application of enzymes. In this study, a structure-based rational design approach was used to improve the thermostability of a highly active, wide-pH-range-adaptable, and stable endopolygalacturonase (PG8fn) from Achaetomium sp. strain Xz8 via the optimization of charge-charge interactions. By using the enzyme thermal stability system (ETSS), two residues-D244 and D299 -were inferred to be crucial contributors to thermostability. Single (D244A and D299R) and double (D244A/D299R) mutants were then generated and compared with the wild type. All mutants showed improved thermal properties, in the order D244A < D299R < D244A/D299R. In comparison with PG8fn, D244A/D299R showed the most pronounced shifts in temperature of maximum enzymatic activity (T max ), temperature at which 50% of the maximal activity of an enzyme is retained (T 50 ), and melting temperature (T m ), of about 10, 17, and 10.2°C upward, respectively, with the half-life (t 1/2 ) extended by 8.4 h at 50°C and 45 min at 55°C. Another distinguishing characteristic of the D244A/D299R mutant was its catalytic activity, which was comparable to that of the wild type (23,000 ؎ 130 U/mg versus 28,000 ؎ 293 U/mg); on the other hand, it showed more residual activity (8,400 ؎ 83 U/mg versus 1,400 ؎ 57 U/mg) after the feed pelleting process (80°C and 30 min). Molecular dynamics (MD) simulation studies indicated that mutations at sites D244 and D299 lowered the overall root mean square deviation (RMSD) and consequently increased the protein rigidity. This study reveals the importance of charge-charge interactions in protein conformation and provides a viable strategy for enhancing protein stability. P ectin, the third most abundant polysaccharide of the plant cell wall, is the most structurally complex polysaccharide consisting of covalently linked galacturonic acid (1, 2). Pectinases-microbial enzymes which are capable of depolymerizing pectinplay an important role in wide biotechnological applications, including the fruit juice, vinification, paper, and textile industries, as well as the extraction of oils (3). Polygalacturonase (PG) is the most widely studied pectinase due to its high activity, mesophilic and acidic properties, and satisfactory performance in juice clarification, extraction, viscosity reduction, and yield improvement (4). Based on sequence similarity and action mode (5), PGs are classified into family 28 of glycoside hydrolase (GH) and endoand exo-types. Most endo-PGs are highly active and stable at 30 to 50°C (6; http://www.brenda-enzymes.org/), which are far from the requirements of thermophilic processing in the feed industry (7).To obtain a thermostable, highly active PG, either mining new genetic resources of thermophiles (8) or engineering the protein and application environment (9, 10) is the most popular practice. Thermophilic fungi Thielavia arenaria XZ7 (60°C) (7), Thermoascus aurantiacus CBMAI-756 (60 to 65°C) (11), Penicillium sp. strain SPC-F 20 (60°C) ...

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High-yield production of a low-temperature-active polygalacturonase for papaya juice clarification

Cited by 71 publications

References 29 publications

Effect of Juicing On Nutrition Qualities of “Sanhua” Plum (Prunus Salicina Lindl.) Juice from 4 Cultivars

Effect of Juicing On Nutrition Qualities of “Sanhua” Plum (Prunus Salicina Lindl.) Juice from 4 Cultivars

Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)

Improvement in Thermostability of an Achaetomium sp. Strain Xz8 Endopolygalacturonase via the Optimization of Charge-Charge Interactions

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