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Characterization of in-situ immobilized laccase-bacteria cellulose biocatalyst: the biocatalyst reusability and decolouration studies / Puvendaran A/L Neelamalai

By:

Puvendaran A/L Neelamalai [author.]

Material type: Text

text

Media type:

unmediated

Carrier type:

volume

ISBN:

THE0010639 (Local)

Subject(s):

Dissertation note: Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2024 Abstract: This research thesis focuses on the characterization of an in-situ immobilized laccase-bacterial cellulose (BC) biocatalyst for its reusability and decolouration efficiency. Enzymes such as laccase have gained significant attention due to their oxidizing capabilities and potential applications in various industries. Immobilization of enzymes enhances their stability, reusability, and catalytic activity. Bacterial cellulose membranes have been widely used as supports for laccase immobilization, offering advantages such as high mechanical strength and a three-dimensional nanostructure. The objective of this study is to determine the reusability of the in-situ immobilized laccase-BC biocatalyst and characterize its decolouration efficiency. Reusability evaluated by studying laccase activity and relative activity over 8 cycles using ABTS as the substrate. The relative activity of the immobilized laccase was observed to be almost 100% in first 3 cycles, more than 60% until 7th cycle and dropping to around 30% in 8th cycle. The decolouration of fruit juice carried out using the immobilized laccase-BC biocatalyst, and the efficiency of decolouration assessed through measurements of juice clarity, colour, and total phenolic content. When using a piece of immobilized laccase, it removed 6% of initial colour and around 12% turbidity. When 2 pieces of immobilized laccases were used, it removed only 4% colour but around 20% turbidity and finally the outcomes of using 3 pieces of immobilized laccases could only remove about 0.9% of colour and 30% of initial turbidity. The findings of this research will contribute to a better understanding of the reusability and decolouration efficiency of the immobilized laccase-BC biocatalyst. This knowledge valuable for the industrial application of the biocatalyst, offering a more sustainable and efficient approach for fruit juice treatment and providing insights into the development of eco-friendly processes in various industries.

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Holdings
Item type	Current library	Call number	Status	Date due	Barcode
Restricted Collection	UMPLIB GAMBANG	FTKKP .P88 2024 r Bc. (Browse shelf(Opens below))	Not for loan		T000004182

Faculty of Chemical and Process Engineering Technology

Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2024

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This research thesis focuses on the characterization of an in-situ immobilized laccase-bacterial cellulose (BC) biocatalyst for its reusability and decolouration efficiency. Enzymes such as laccase have gained significant attention due to their oxidizing capabilities and potential applications in various industries. Immobilization of enzymes enhances their stability, reusability, and catalytic activity. Bacterial cellulose membranes have been widely used as supports for laccase immobilization, offering advantages such as high mechanical strength and a three-dimensional nanostructure. The objective of this study is to determine the reusability of the in-situ immobilized laccase-BC biocatalyst and characterize its decolouration efficiency. Reusability evaluated by studying laccase activity and relative activity over 8 cycles using ABTS as the substrate. The relative activity of the immobilized laccase was observed to be almost 100% in first 3 cycles, more than 60% until 7th cycle and dropping to around 30% in 8th cycle. The decolouration of fruit juice carried out using the immobilized laccase-BC biocatalyst, and the efficiency of decolouration assessed through measurements of juice clarity, colour, and total phenolic content. When using a piece of immobilized laccase, it removed 6% of initial colour and around 12% turbidity. When 2 pieces of immobilized laccases were used, it removed only 4% colour but around 20% turbidity and finally the outcomes of using 3 pieces of immobilized laccases could only remove about 0.9% of colour and 30% of initial turbidity. The findings of this research will contribute to a better understanding of the reusability and decolouration efficiency of the immobilized laccase-BC biocatalyst. This knowledge valuable for the industrial application of the biocatalyst, offering a more sustainable and efficient approach for fruit juice treatment and providing insights into the development of eco-friendly processes in various industries.