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Purification and Characterization of Bromelain from Waste Parts of Ananas comosus for its Application in Detergent Industry

Purification and Characterization of Bromelain from Waste Parts of Ananas comosus for its Application in Detergent Industry

Fariha Javaid1*, Zahoor Qadir Samra1, Madeeha Shahzad Lodhi1,2, Aroosha Hussain1 and Gulnaz Pervaiz1

1School of Biochemistry and Biotechnology, University of the Punjab, Quaid-i-Azam Campus, Lahore, Punjab
2Institute of Molecular Biology and Biotechnology, The University of Lahore, 1-Km Defence Road, Near Bhuptian Chowk, Lahore, Punjab
 
* Corresponding author: javaid.fariha@hotmail.com

ABSTRACT

Bromelain is a thiol-containing cysteine protease isolated from the stem, peel, and leaf parts of Ananas comosus. Protease accounts for 60% of the total enzyme market. Being a plant-based cysteine protease, it has various pharmaceutical and biotechnological applications. The isolation and purification cost of the enzyme is highest, so there is a need to develop cost-effective purification methods. This research work aims to purify BRM by using magnetic nanoparticles. After purification, BRM enzyme was characterized and utilized in the detergent industry due to its stability at a wide range of pH and temperature; results showed that stem BRM has the highest enzyme activity at 23.5 U/ml as compared to crown leaf (11.7 U/ml) and peel (19.5 U/ml). The specific activity of leaf, peel, and stem BRM was determined 0.8, 1.2, and 1.4 U/mg, respectively. Total protein content was 660 mg, 810 mg, and 865 mg from leaf, peel, and stem samples. The percentage yield of BRM was determined in the range of 60 to 93 % from these waste parts of the plant. This study achieved 4, 6, and 7-fold purification for leaf, peel, and stem BRM, respectively. This study showed positive results for utilizing affinity-purified BRM enzyme in the laundry and detergent industry due to its stability in different detergents and destaining properties.

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Pakistan Journal of Zoology

April

Pakistan J. Zool., Vol. 56, Iss. 2, pp. 503-1000

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