Doctor of Philosophy
Aziana Abu Hassan
Malaysian Rubber Board, RRIM Research Station, 47000 Sungai Buloh, Selangor, Malaysia
Title: Structure and Property Transformations During LcpK30-Catalyzed Degradation of Natural Rubber Latex
Aziana Abu Hassan, Nurulhuda Abdullah, Nurul Hayati Yusof and Shabinah Filza
The modification of natural rubber (NR) is essential for producing new functional materials such as liquid natural rubber (LNR), which can serve as adhesives, coatings, or reactive plasticizers. However, conventional chemical degradation methods often require harsh reagents, long reaction times, and high temperatures, while generating significant waste and offering limited control over molecular weight and end-group functionality. These challenges highlight the need for greener, biotechnology-driven approaches to NR modification. Enzymes such as microbial rubber oxygenase LcpK30 offer a sustainable alternative, yet their activity on different latex substrates, particularly freshly tapped latex (FL) versus commercial high-ammoniated latex (HA), remains insufficiently characterized. This study investigates the biodegradation of NR latex by LcpK30 using FL and HA as substrates to understand substrate-dependent enzymatic behaviour. Enzymatic activity was verified using Schiff’s reagent, which detected aldehyde-containing degradation products. Dynamic light scattering revealed distinct fragmentation patterns, with FL treated with LcpK30 (FL+E) transitioning to a uniform particle size distribution of 4–5 µm, whereas HA treated with LcpK30 (HA+E) showed rapid size reduction (2–4 µm) followed by secondary aggregation. Zeta potential measurements indicated transient charge perturbations during degradation, stabilizing by day three. Gel content and GPC analyses confirmed extensive polyisoprene cleavage. FL+E exhibited a drastic reduction in molecular weight (Mw 2134×10³ to 39×10³ g/mol), while HA+E showed reduced crosslink density. Oligomer yields of 26.5–31.5% demonstrated efficient enzymatic depolymerization for both substrates. Overall, these findings establish LcpK30 as an effective oxidative biocatalyst capable of converting NR latex into functional low-molecular-weight oligomers. The enzyme’s performance strongly depends on the physicochemical nature of the latex substrate, with FL showing greater post-degradation stability. This work supports the potential of enzyme-based strategies for sustainable rubber recycling and greener polymer modification.
Biography of the presenting author
Dr. Aziana holds a PhD in Biotechnology (Engineering) from the University of Nottingham, UK, and has served as a Research Officer at the Malaysian Rubber Board (MRB) since 2007. Her work centres on applied and microbial biotechnology with a strong focus on integrating biological approaches into natural rubber latex (NRL) processing to drive industry innovation and sustainability. Her research portfolio includes studies on endotoxins, NRL deproteinization, and microbial or enzymatic biodegradation of natural rubber. She is also actively involved in assessing the antimicrobial properties of rubber products and provides consultation, laboratory analysis, and testing services to support industrial stakeholders. Beyond research, Dr. Aziana contributes to capacity building and professional training within the rubber sector. She is a regular lecturer for the Latex Science and Technology Course, delivering modules on allergens, endotoxins, and antimicrobial performance. She also frequently represents MRB at national and international conferences, sharing scientific advancements and strengthening knowledge exchange within the global rubber community.
Presenting author details
Full name: Dr Aziana Abu Hassan
Contact number: +6 0126432803
Email: aziana@lgm.gov.my
ResearcherID:-
ORCID: 0000-0002-2206-0149
Session name/ number: Industrial/Environmental Biotechnology
Category: Oral presentation