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Laccase immobilization onto oxidized bacterial cellulose: the effect of oxidant and its oxidation degree analysis / Yashini Devi A/P Subramaniam

By:

Yashini Devi A/P Subramaniam, , [author.]

Material type: Text

text

Media type:

unmediated

Carrier type:

volume

ISBN:

THE0010724 (Local)

Subject(s):

Dissertation note: Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025 Abstract: Laccases, a subgroup of multicopper oxidases, play a crucial role in biotechnological applications but face limitations such as low stability, poor reusability, and recovery challenges. This study investigates the effects of oxidant to Bacterial Cellulose (BC) weight ratio and sodium periodate (NaIO4) concentration on oxidation degree (OD) and laccase immobilization efficiency to determine best condition for enzyme stability and activity. The results indicate that increasing the oxidant to BC ratio from 0.02:1 to 0.06:1 led to a gradual increase in OD, peaking at 12.3%, while further increments resulted in over oxidation, causing structural degradation and reduced immobilization efficiency. Similarly, NaIO4 concentrations between 0.2% and 0.6% improved enzyme binding by enhancing aldehyde functionalities, but concentrations beyond 0.6% led to excessive oxidation and mass loss, negatively impacting enzyme stability. Under best condition of 0.06:1 oxidant to BC ratio and 0.6% NaIO4 concentration, Oxidized Bacterial Cellulose (OxBC) demonstrated superior immobilization performance, achieving a laccase activity of 0.04 U, with a recovered activity of 0.2%, and bound laccase of 17.0 U/g of support. The aldehyde groups introduced through oxidation facilitated stable covalent binding, significantly improving enzyme retention and reusability. Compared to native BC, OxBC exhibited enhanced immobilization efficiency and structural integrity, making it a promising candidate for industrial enzyme applications. This study provides insight into the relationship between oxidation parameters and immobilization efficiency, contributing to the development of more effective and sustainable enzyme immobilization systems. Future research should explore long term operational stability and scalability of OxBC based immobilization for broader industrial and environmental applications.

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Holdings
Item type	Current library	Call number	Status	Date due	Barcode
Restricted Collection	UMPLIB GAMBANG	FTKKP .Y37 2025 r Bc. (Browse shelf(Opens below))	Not for loan		T000004317

Faculty of Chemical and Process Engineering Technology

Final Year Report (Bachelor of Chemical Engineering ) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025

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Laccases, a subgroup of multicopper oxidases, play a crucial role in biotechnological applications but face limitations such as low stability, poor reusability, and recovery challenges. This study investigates the effects of oxidant to Bacterial Cellulose (BC) weight ratio and sodium periodate (NaIO4) concentration on oxidation degree (OD) and laccase immobilization efficiency to determine best condition for enzyme stability and activity. The results indicate that increasing the oxidant to BC ratio from 0.02:1 to 0.06:1 led to a gradual increase in OD, peaking at 12.3%, while further increments resulted in over oxidation, causing structural degradation and reduced immobilization efficiency. Similarly, NaIO4 concentrations between 0.2% and 0.6% improved enzyme binding by enhancing aldehyde functionalities, but concentrations beyond 0.6% led to excessive oxidation and mass loss, negatively impacting enzyme stability. Under best condition of 0.06:1 oxidant to BC ratio and 0.6% NaIO4 concentration, Oxidized Bacterial Cellulose (OxBC) demonstrated superior immobilization performance, achieving a laccase activity of 0.04 U, with a recovered activity of 0.2%, and bound laccase of 17.0 U/g of support. The aldehyde groups introduced through oxidation facilitated stable covalent binding, significantly improving enzyme retention and reusability. Compared to native BC, OxBC exhibited enhanced immobilization efficiency and structural integrity, making it a promising candidate for industrial enzyme applications. This study provides insight into the relationship between oxidation parameters and immobilization efficiency, contributing to the development of more effective and sustainable enzyme immobilization systems. Future research should explore long term operational stability and scalability of OxBC based immobilization for broader industrial and environmental applications.