A comparative study of polyphenoloxidases from taro (Colocasia esculenta) and potato (Solanum tuberosum var. Romano

K Duangmal, Richard Owusu-Apenten

Research output: Contribution to journalArticle

135 Citations (Scopus)

Abstract

Taro (C. esculenta) is a staple food in many tropical regions. A comparative study of crude polyphenoloxidases from tare (tPPO) and potatoes (pPPO) was carried out to provide information useful for guiding food processing operations. Crude PPO was prepared by cold acetone precipitation using ascorbic acid as antioxidant. The PPO content of tare acetone powder was 770 +/- 17 units (mg protein)(-1) as compared with 3848 +/- 180 units (mg protein)(-1) in potato acetone powder. The pH-activity optimum was pH 4.6 for tPPO and pH 6.8 for pPPO. Both enzymes retained > 80% activity after incubation at pH 4.5-8 but there was rapid activity loss at pH <4. The temperature-activity optimum (T-opt) was 30 degrees C for tPPO and 25 degrees C for pPPO with 75 and 27% of their respective maximum activity retained at 60 degrees C. Both tPPO and pPPO were irreversibly inactivated by 10 min heating at 70 degrees C. The activation enthalpy (Delta H-#) and activation entropy (Delta S-#) for tPPO heat-inactivation were 87.4 (+/-0.1) kJ mol(-1) and -56.2 (+/-4) J mol(-1) K-1, respectively. For pPPO, Delta H-# was 59.1 (+/- 0.1) kJ mol(-1) whilst Delta S-# was -141 (+/- 4) J mol(-1) K-1. The apparent substrate specificity was established from values V-max/K-m, as: 4-methylcatechol > chlorogenic acid > DL-dopa > catechol > pyrogallol > dopamine > > caffeic acid for tPPO. There was no detectable activity towards caffeic acid. The substrate specificity for pPPO was: 4-methylcatechol > caffeic acid > pyrogallol > catechol > chlorogenic acid > DL-dopa > dopamine. According to the order of inhibitor effectiveness (sodium metabisulphite > ascorbic acid > NaCl approximate to (EDTA), there was a significant lag-phase before increases occurred in the absorbance at 420 nm. Preincubation of PPO with inhibitors increased the extent of inhibition, indicating a direct effect on the structure of the enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.
LanguageEnglish
Pages351-359
JournalFood Chemistry
Volume64
Issue number3
DOIs
Publication statusPublished - 1 Feb 1999

Fingerprint

Colocasia
Catechol Oxidase
Polyphenylene oxides
taro
Colocasia esculenta
Solanum tuberosum
Acetone
catechol oxidase
Pyrogallol
Chlorogenic Acid
Dihydroxyphenylalanine
potatoes
caffeic acid
Powders
Ascorbic Acid
Dopamine
acetone
pyrogallol
catechol
chlorogenic acid

Cite this

@article{e8cd2f419508456c84903f1884f0e2cc,
title = "A comparative study of polyphenoloxidases from taro (Colocasia esculenta) and potato (Solanum tuberosum var. Romano",
abstract = "Taro (C. esculenta) is a staple food in many tropical regions. A comparative study of crude polyphenoloxidases from tare (tPPO) and potatoes (pPPO) was carried out to provide information useful for guiding food processing operations. Crude PPO was prepared by cold acetone precipitation using ascorbic acid as antioxidant. The PPO content of tare acetone powder was 770 +/- 17 units (mg protein)(-1) as compared with 3848 +/- 180 units (mg protein)(-1) in potato acetone powder. The pH-activity optimum was pH 4.6 for tPPO and pH 6.8 for pPPO. Both enzymes retained > 80{\%} activity after incubation at pH 4.5-8 but there was rapid activity loss at pH <4. The temperature-activity optimum (T-opt) was 30 degrees C for tPPO and 25 degrees C for pPPO with 75 and 27{\%} of their respective maximum activity retained at 60 degrees C. Both tPPO and pPPO were irreversibly inactivated by 10 min heating at 70 degrees C. The activation enthalpy (Delta H-#) and activation entropy (Delta S-#) for tPPO heat-inactivation were 87.4 (+/-0.1) kJ mol(-1) and -56.2 (+/-4) J mol(-1) K-1, respectively. For pPPO, Delta H-# was 59.1 (+/- 0.1) kJ mol(-1) whilst Delta S-# was -141 (+/- 4) J mol(-1) K-1. The apparent substrate specificity was established from values V-max/K-m, as: 4-methylcatechol > chlorogenic acid > DL-dopa > catechol > pyrogallol > dopamine > > caffeic acid for tPPO. There was no detectable activity towards caffeic acid. The substrate specificity for pPPO was: 4-methylcatechol > caffeic acid > pyrogallol > catechol > chlorogenic acid > DL-dopa > dopamine. According to the order of inhibitor effectiveness (sodium metabisulphite > ascorbic acid > NaCl approximate to (EDTA), there was a significant lag-phase before increases occurred in the absorbance at 420 nm. Preincubation of PPO with inhibitors increased the extent of inhibition, indicating a direct effect on the structure of the enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.",
author = "K Duangmal and Richard Owusu-Apenten",
note = "Reference text: 1. ABUKHARMA DA PREPARATION AND PROPERTIES OF O-DIPHENOL - OXYGEN OXIDOREDUCTASE FROM POTATO TUBERS NEW PHYTOLOGIST 65 : 477 1966 2. ALBERGHINA FAM CHLOROGENIC ACID OXIDASE FROM POTATO TUBER SLICES - PARTIAL PURIFICATION AND PROPERTIES PHYTOCHEMISTRY 3 : 65 1964 3. AMIOT MJ INFLUENCE OF CULTIVAR, MATURITY STAGE, AND STORAGE-CONDITIONS ON PHENOLIC COMPOSITION AND ENZYMATIC BROWNING OF PEAR FRUITS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 43 : 1132 1995 4. AMIZA MA THERMAL INACTIVATION PARAMETERS FOR ALKALINE PROTEINASES FROM NORTH-SEA COD (GADUS-MORHUA) AND BOVINE ALPHA-CHYMOTRYPSIN JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 66 : 389 1994 5. ANOSIKE EO PURIFICATION AND SOME PROPERTIES OF POLYPHENOL OXIDASE FROM THE YAM TUBERS, DIOSCOREA-BULBIFERA PHYTOCHEMISTRY 20 : 2625 1981 6. ASEMOTA HN EFFECT OF SHORT-TERM STORAGE ON PHENOLIC CONTENT, O-DIPHENOLASE AND PEROXIDASE-ACTIVITIES OF CUT YAM TUBERS (DIOSCOREA SP) JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 60 : 309 1992 7. BENJAMIN ND POLYPHENOL OXIDASE OF ROYAL ANN CHERRIES - PURIFICATION AND CHARACTERIZATION JOURNAL OF FOOD SCIENCE 38 : 799 1973 8. EMBS RJ MECHANISM OF SULFITE INHIBITION OF BROWNING CAUSED BY POLYPHENOL OXIDASE JOURNAL OF FOOD SCIENCE 30 : 753 1965 9. GALANI D The comparative heat stability of bovine beta-lactoglobulin in buffer and complex media JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 74 : 89 1997 10. GOLANGOLDHIRSH A EFFECT OF ASCORBIC-ACID, SODIUM BISULFITE, AND THIOL COMPOUNDS ON MUSHROOM POLYPHENOL OXIDASE JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 32 : 1003 1984 11. HALIM DH POLYPHENOL OXIDASE OF DANJOU PEARS (PYRUS-COMMUNIS L) JOURNAL OF FOOD SCIENCE 43 : 603 1978 12. IYENGAR R TRENDS FOOD SCI TECH 3 : 60 1992 13. LAMIKANRA O ENZYMATIC BROWNING OF MUSCADINE GRAPE PRODUCTS ENZYMATIC BROWNING AND ITS PREVENTION 600 : 166 1995 14. LEE CY ENZYMATIC BROWNING IN RELATION TO PHENOLIC-COMPOUNDS AND POLYPHENOLOXIDASE ACTIVITY AMONG VARIOUS PEACH CULTIVARS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 38 : 99 1990 15. LOURENCO EJ POLYPHENOL OXIDASE FROM SWEET-POTATO - PURIFICATION AND PROPERTIES JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 40 : 2369 1992 16. LUH BS CHARACTERISTICS OF POLYPHENOLOXIDASE RELATED TO BROWNING IN CLING PEACHES JOURNAL OF FOOD SCIENCE 37 : 264 1972 17. MARTINEZ MV THE BIOCHEMISTRY AND CONTROL OF ENZYMATIC BROWNING TRENDS IN FOOD SCIENCE & TECHNOLOGY 6 : 195 1995 18. MATHEIS G CHEM MIKROBIOL TECHN 11 : 5 1987 19. MATHEIS G CHEM MIKROBIOL TECHN 11 : 33 1987 20. MEGA JA FOOD REV INT 8 : 443 1992 21. NGALANI JA PARTIAL-PURIFICATION AND PROPERTIES OF PLANTAIN POLYPHENOL OXIDASE FOOD CHEMISTRY 48 : 341 1993 22. PALMER T UNDERSTANDING ENZYME : 107 1995 23. PATIL SS POTATO PHENOLASES JOURNAL OF BIOLOGICAL CHEMISTRY 240 : 3938 1965 24. PETERSON GL SIMPLIFICATION OF PROTEIN ASSAY METHOD OF LOWRY ET AL - WHICH IS MORE GENERALLY APPLICABLE ANALYTICAL BIOCHEMISTRY 83 : 346 1977 25. RAVI V Review on tropical root and tuber crops .1. Storage methods and quality changes CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION 36 : 661 1996 26. RHEE JK HISTOLOGICAL OBSERVATIONS ON THE CHILLING INJURY OF TARO TUBERS DURING COLD-STORAGE JOURNAL OF THE JAPANESE SOCIETY FOR HORTICULTURAL SCIENCE 51 : 362 1982 27. SAPERS GM BROWNING OF FOODS - CONTROL BY SULFITES, ANTIOXIDANTS, AND OTHER MEANS FOOD TECHNOLOGY 47 : 75 1993 28. SAPERS GM ENZYMATIC BROWNING IN ATLANTIC POTATOES AND RELATED CULTIVARS JOURNAL OF FOOD SCIENCE 54 : 362 1989 29. SAYAVEDRASOTO LA INHIBITION OF POLYPHENOLOXIDASE BY SULFITE JOURNAL OF FOOD SCIENCE 51 : 1531 1986 30. SHIOTA Y J FOOD SCI TECHNOL J 15 : 547 1968 31. VAMOSVIGYAZO L POLYPHENOL OXIDASE AND PEROXIDASE IN FRUITS AND VEGETABLES CRC CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION 15 : 49 1981 32. WALKER JRL ENZYMATIC BROWNING IN FRUITS - ITS BIOCHEMISTRY AND CONTROL ENZYMATIC BROWNING AND ITS PREVENTION 600 : 8 1995 33. WALTER WM EFFECT OF SUBSTRATE LEVELS AND POLYPHENOL OXIDASE ACTIVITY ON DARKENING IN SWEET-POTATO CULTIVARS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 28 : 941 1980 34. WHITAKER JR RECENT ADVANCES IN CHEMISTRY OF ENZYMATIC BROWNING - AN OVERVIEW ENZYMATIC BROWNING AND ITS PREVENTION 600 : 2 1995 35. WHITAKER JR PRINCIPLES ENZYMOLOG : 241 1994 36. ZAWISTOWSKI J OXIDATIVE ENZYMES FO : 217 1991",
year = "1999",
month = "2",
day = "1",
doi = "10.1016/S0308-8146(98)00127-7",
language = "English",
volume = "64",
pages = "351--359",
journal = "Food Chemistry",
issn = "0308-8146",
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}

A comparative study of polyphenoloxidases from taro (Colocasia esculenta) and potato (Solanum tuberosum var. Romano. / Duangmal, K; Owusu-Apenten, Richard.

In: Food Chemistry, Vol. 64, No. 3, 01.02.1999, p. 351-359.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A comparative study of polyphenoloxidases from taro (Colocasia esculenta) and potato (Solanum tuberosum var. Romano

AU - Duangmal, K

AU - Owusu-Apenten, Richard

N1 - Reference text: 1. ABUKHARMA DA PREPARATION AND PROPERTIES OF O-DIPHENOL - OXYGEN OXIDOREDUCTASE FROM POTATO TUBERS NEW PHYTOLOGIST 65 : 477 1966 2. ALBERGHINA FAM CHLOROGENIC ACID OXIDASE FROM POTATO TUBER SLICES - PARTIAL PURIFICATION AND PROPERTIES PHYTOCHEMISTRY 3 : 65 1964 3. AMIOT MJ INFLUENCE OF CULTIVAR, MATURITY STAGE, AND STORAGE-CONDITIONS ON PHENOLIC COMPOSITION AND ENZYMATIC BROWNING OF PEAR FRUITS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 43 : 1132 1995 4. AMIZA MA THERMAL INACTIVATION PARAMETERS FOR ALKALINE PROTEINASES FROM NORTH-SEA COD (GADUS-MORHUA) AND BOVINE ALPHA-CHYMOTRYPSIN JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 66 : 389 1994 5. ANOSIKE EO PURIFICATION AND SOME PROPERTIES OF POLYPHENOL OXIDASE FROM THE YAM TUBERS, DIOSCOREA-BULBIFERA PHYTOCHEMISTRY 20 : 2625 1981 6. ASEMOTA HN EFFECT OF SHORT-TERM STORAGE ON PHENOLIC CONTENT, O-DIPHENOLASE AND PEROXIDASE-ACTIVITIES OF CUT YAM TUBERS (DIOSCOREA SP) JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 60 : 309 1992 7. BENJAMIN ND POLYPHENOL OXIDASE OF ROYAL ANN CHERRIES - PURIFICATION AND CHARACTERIZATION JOURNAL OF FOOD SCIENCE 38 : 799 1973 8. EMBS RJ MECHANISM OF SULFITE INHIBITION OF BROWNING CAUSED BY POLYPHENOL OXIDASE JOURNAL OF FOOD SCIENCE 30 : 753 1965 9. GALANI D The comparative heat stability of bovine beta-lactoglobulin in buffer and complex media JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE 74 : 89 1997 10. GOLANGOLDHIRSH A EFFECT OF ASCORBIC-ACID, SODIUM BISULFITE, AND THIOL COMPOUNDS ON MUSHROOM POLYPHENOL OXIDASE JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 32 : 1003 1984 11. HALIM DH POLYPHENOL OXIDASE OF DANJOU PEARS (PYRUS-COMMUNIS L) JOURNAL OF FOOD SCIENCE 43 : 603 1978 12. IYENGAR R TRENDS FOOD SCI TECH 3 : 60 1992 13. LAMIKANRA O ENZYMATIC BROWNING OF MUSCADINE GRAPE PRODUCTS ENZYMATIC BROWNING AND ITS PREVENTION 600 : 166 1995 14. LEE CY ENZYMATIC BROWNING IN RELATION TO PHENOLIC-COMPOUNDS AND POLYPHENOLOXIDASE ACTIVITY AMONG VARIOUS PEACH CULTIVARS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 38 : 99 1990 15. LOURENCO EJ POLYPHENOL OXIDASE FROM SWEET-POTATO - PURIFICATION AND PROPERTIES JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 40 : 2369 1992 16. LUH BS CHARACTERISTICS OF POLYPHENOLOXIDASE RELATED TO BROWNING IN CLING PEACHES JOURNAL OF FOOD SCIENCE 37 : 264 1972 17. MARTINEZ MV THE BIOCHEMISTRY AND CONTROL OF ENZYMATIC BROWNING TRENDS IN FOOD SCIENCE & TECHNOLOGY 6 : 195 1995 18. MATHEIS G CHEM MIKROBIOL TECHN 11 : 5 1987 19. MATHEIS G CHEM MIKROBIOL TECHN 11 : 33 1987 20. MEGA JA FOOD REV INT 8 : 443 1992 21. NGALANI JA PARTIAL-PURIFICATION AND PROPERTIES OF PLANTAIN POLYPHENOL OXIDASE FOOD CHEMISTRY 48 : 341 1993 22. PALMER T UNDERSTANDING ENZYME : 107 1995 23. PATIL SS POTATO PHENOLASES JOURNAL OF BIOLOGICAL CHEMISTRY 240 : 3938 1965 24. PETERSON GL SIMPLIFICATION OF PROTEIN ASSAY METHOD OF LOWRY ET AL - WHICH IS MORE GENERALLY APPLICABLE ANALYTICAL BIOCHEMISTRY 83 : 346 1977 25. RAVI V Review on tropical root and tuber crops .1. Storage methods and quality changes CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION 36 : 661 1996 26. RHEE JK HISTOLOGICAL OBSERVATIONS ON THE CHILLING INJURY OF TARO TUBERS DURING COLD-STORAGE JOURNAL OF THE JAPANESE SOCIETY FOR HORTICULTURAL SCIENCE 51 : 362 1982 27. SAPERS GM BROWNING OF FOODS - CONTROL BY SULFITES, ANTIOXIDANTS, AND OTHER MEANS FOOD TECHNOLOGY 47 : 75 1993 28. SAPERS GM ENZYMATIC BROWNING IN ATLANTIC POTATOES AND RELATED CULTIVARS JOURNAL OF FOOD SCIENCE 54 : 362 1989 29. SAYAVEDRASOTO LA INHIBITION OF POLYPHENOLOXIDASE BY SULFITE JOURNAL OF FOOD SCIENCE 51 : 1531 1986 30. SHIOTA Y J FOOD SCI TECHNOL J 15 : 547 1968 31. VAMOSVIGYAZO L POLYPHENOL OXIDASE AND PEROXIDASE IN FRUITS AND VEGETABLES CRC CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION 15 : 49 1981 32. WALKER JRL ENZYMATIC BROWNING IN FRUITS - ITS BIOCHEMISTRY AND CONTROL ENZYMATIC BROWNING AND ITS PREVENTION 600 : 8 1995 33. WALTER WM EFFECT OF SUBSTRATE LEVELS AND POLYPHENOL OXIDASE ACTIVITY ON DARKENING IN SWEET-POTATO CULTIVARS JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 28 : 941 1980 34. WHITAKER JR RECENT ADVANCES IN CHEMISTRY OF ENZYMATIC BROWNING - AN OVERVIEW ENZYMATIC BROWNING AND ITS PREVENTION 600 : 2 1995 35. WHITAKER JR PRINCIPLES ENZYMOLOG : 241 1994 36. ZAWISTOWSKI J OXIDATIVE ENZYMES FO : 217 1991

PY - 1999/2/1

Y1 - 1999/2/1

N2 - Taro (C. esculenta) is a staple food in many tropical regions. A comparative study of crude polyphenoloxidases from tare (tPPO) and potatoes (pPPO) was carried out to provide information useful for guiding food processing operations. Crude PPO was prepared by cold acetone precipitation using ascorbic acid as antioxidant. The PPO content of tare acetone powder was 770 +/- 17 units (mg protein)(-1) as compared with 3848 +/- 180 units (mg protein)(-1) in potato acetone powder. The pH-activity optimum was pH 4.6 for tPPO and pH 6.8 for pPPO. Both enzymes retained > 80% activity after incubation at pH 4.5-8 but there was rapid activity loss at pH <4. The temperature-activity optimum (T-opt) was 30 degrees C for tPPO and 25 degrees C for pPPO with 75 and 27% of their respective maximum activity retained at 60 degrees C. Both tPPO and pPPO were irreversibly inactivated by 10 min heating at 70 degrees C. The activation enthalpy (Delta H-#) and activation entropy (Delta S-#) for tPPO heat-inactivation were 87.4 (+/-0.1) kJ mol(-1) and -56.2 (+/-4) J mol(-1) K-1, respectively. For pPPO, Delta H-# was 59.1 (+/- 0.1) kJ mol(-1) whilst Delta S-# was -141 (+/- 4) J mol(-1) K-1. The apparent substrate specificity was established from values V-max/K-m, as: 4-methylcatechol > chlorogenic acid > DL-dopa > catechol > pyrogallol > dopamine > > caffeic acid for tPPO. There was no detectable activity towards caffeic acid. The substrate specificity for pPPO was: 4-methylcatechol > caffeic acid > pyrogallol > catechol > chlorogenic acid > DL-dopa > dopamine. According to the order of inhibitor effectiveness (sodium metabisulphite > ascorbic acid > NaCl approximate to (EDTA), there was a significant lag-phase before increases occurred in the absorbance at 420 nm. Preincubation of PPO with inhibitors increased the extent of inhibition, indicating a direct effect on the structure of the enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.

AB - Taro (C. esculenta) is a staple food in many tropical regions. A comparative study of crude polyphenoloxidases from tare (tPPO) and potatoes (pPPO) was carried out to provide information useful for guiding food processing operations. Crude PPO was prepared by cold acetone precipitation using ascorbic acid as antioxidant. The PPO content of tare acetone powder was 770 +/- 17 units (mg protein)(-1) as compared with 3848 +/- 180 units (mg protein)(-1) in potato acetone powder. The pH-activity optimum was pH 4.6 for tPPO and pH 6.8 for pPPO. Both enzymes retained > 80% activity after incubation at pH 4.5-8 but there was rapid activity loss at pH <4. The temperature-activity optimum (T-opt) was 30 degrees C for tPPO and 25 degrees C for pPPO with 75 and 27% of their respective maximum activity retained at 60 degrees C. Both tPPO and pPPO were irreversibly inactivated by 10 min heating at 70 degrees C. The activation enthalpy (Delta H-#) and activation entropy (Delta S-#) for tPPO heat-inactivation were 87.4 (+/-0.1) kJ mol(-1) and -56.2 (+/-4) J mol(-1) K-1, respectively. For pPPO, Delta H-# was 59.1 (+/- 0.1) kJ mol(-1) whilst Delta S-# was -141 (+/- 4) J mol(-1) K-1. The apparent substrate specificity was established from values V-max/K-m, as: 4-methylcatechol > chlorogenic acid > DL-dopa > catechol > pyrogallol > dopamine > > caffeic acid for tPPO. There was no detectable activity towards caffeic acid. The substrate specificity for pPPO was: 4-methylcatechol > caffeic acid > pyrogallol > catechol > chlorogenic acid > DL-dopa > dopamine. According to the order of inhibitor effectiveness (sodium metabisulphite > ascorbic acid > NaCl approximate to (EDTA), there was a significant lag-phase before increases occurred in the absorbance at 420 nm. Preincubation of PPO with inhibitors increased the extent of inhibition, indicating a direct effect on the structure of the enzyme. (C) 1998 Elsevier Science Ltd. All rights reserved.

U2 - 10.1016/S0308-8146(98)00127-7

DO - 10.1016/S0308-8146(98)00127-7

M3 - Article

VL - 64

SP - 351

EP - 359

JO - Food Chemistry

T2 - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

IS - 3

ER -