Follow
International Journal of Current Microbiology and Applied Sciences (IJCMAS)
IJCMAS is now DOI (CrossRef) registered Research Journal. The DOIs are assigned to all published IJCMAS Articles.
Index Copernicus ICI Journals Master List 2018 - IJCMAS--ICV 2018: 95.39 For more details click here
National Academy of Agricultural Sciences (NAAS) : NAAS Score: *5.38 (2019) [Effective from January 1, 2019]For more details click here

Login as a Reviewer

Indexed in



National Academy of Agricultural Sciences (NAAS)
NAAS Score: *5.38 (2019)
[Effective from January 1, 2019]
For more details click here

ICV 2018: 95.39
Index Copernicus ICI Journals Master List 2017 - IJCMAS--ICV 2018: 95.39
For more details click here

See Guidelines to Authors
Current Issues

Original Research Articles

PRINT ISSN : 2319-7692
Online ISSN : 2319-7706
Issues : 12 per year
Publisher : Excellent Publishers
Email : editorijcmas@gmail.com / submit@ijcmas.com
Editor-in-chief: Dr.M.Prakash
Index Copernicus ICV 2017: 100.00
NAAS RATING 2018: 5.38

Int.J.Curr.Microbiol.App.Sci.2017.6(6): 2729-2739
DOI: https://doi.org/10.20546/ijcmas.2017.606.326


Partial purification and Characterization of Two Pectinases (Polygalacturonase and Pectin lyase) from Papaya Pericarp (Carica papaya cv. solo 8)
Adingra Kouassi Martial-Didier1, Konan Kouassi Hubert2*, Kouadio Eugène Jean Parfait2, Yapi Jocelyn Constant2 and Tano Kablan1
1Laboratoire de Biochimie Alimentaire et de Technologie des Produits Tropicaux de l’Université Nangui Abrogoua (Abidjan, Côte d’Ivoire), 02 BP 801 Abidjan 02, Côte d’Ivoire
2Laboratoire de Biocatalyse et des Bioprocédés de l’Université Nangui Abrogoua (Abidjan, Côte d’Ivoire), 02 BP 801 Abidjan 02, Côte d’Ivoire
*Corresponding author
Abstract:

Plant wastes could be a potential source of novel pectinases for use in various industrial applications due to their broad substrate specificity with high stability under extreme conditions. Therefore, the application conditions of novel pectinases (Polygalacturonase and Pectin lyase) from Carica papaya cv. solo 8 pericarp were optimized in this study. Those enzymes were partially purified by ammonium sulphate precipitation, dialysis and isoelectric focusing. The polygalacturonase and pectin lyase were partially purified 1.3 and 1.26 fold with a yield approximately 20 % and 24 %, respectively, following purification with isoelectric focusing. The specific activities of 3.62 and 0.176 UI/mg for polygalacturonase and pectin lyase enzymes were calculated, respectively. The optimal pH of 5.0 and 8.0 were obtained for the polygalacturonase and pectin lyase, respectively while an optimal temperature of 45°C was obtained for polygalacturonase and 50 °C for pectin lyase. Polygalacturonase and pectin lyase activities were enhanced by Na+, Ca2+, K+, and Mg2+ while EDTA has any effect at all concentrations on pectin lyase activity whereas EDTA was inhibitory to polygalacturonase activity. The results suggest that Carica papaya pericarp peels can be used for value added synthesis of pectinase, an important enzyme with numerous biotechnological applications.


Keywords: Biochemical properties, Carica papaya, Pericarp, Polygalacturonase, Pectin lyase, Purification.
Download this article as Download

How to cite this article:

Adingra Kouassi Martial-Didier, Konan Kouassi Hubert, Kouadio Eugène Jean Parfait, Yapi Jocelyn Constant and Tano Kablan. 2017. Partial Purification and Characterization of Two Pectinases (Polygalacturonase and Pectin Lyase) from Papaya Pericarp (Carica papaya cv. solo 8).Int.J.Curr.Microbiol.App.Sci. 6(6): 2729-2739. doi: https://doi.org/10.20546/ijcmas.2017.606.326