Browsing by Author "Nur Zazarina Ramly"
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Publication Combining Docking And Molecular Dynamic Of Protease From Bacillus Lehensis G1(RMP Publications, 2018) ;Noorul Aini Sulaiman ;Shuhaila Mat-Sharani ;Nor Muhammad MahadiNur Zazarina RamlyProtease is an enzyme that catalysed the hydrolysis of protein into peptide. Application of protease in industry has been linked with cost effective substrates and complex of enzyme-substrate stability. Molecular docking approach has identified casein as a preference substrates. However, lack of data on casein mode of binding to protease and enzyme stability represents a limitation for its production and structural optimization. In this study, we have used a molecular dynamic (MD) to examine the stability of complex enzyme-substrate of protease from Bacillus lehensis G1. The 3D structure of protease (BleG1_1979) was docked with substrate casein using AutoDock Vina. Structural analysis of the substrate-binding cleft revealed a binding site of casein was predominantly at the hydrophobic region of BleG1_1979. The MD of complex BleG1_1979-casein was tested with two temperatures; 298 K and 310 K using GROMACS v5.1.4. MD simulation showed a stable behaviour of BleG1_1979 over the 20 ns simulation period. The molecular docking and MD simulation suggested that the production of protease from B. lehensis G1 by utilization of casein and the stability of complex protease-casein could be a potential application to generate a cost effective enzyme to be develop for industrial use - Some of the metrics are blocked by yourconsent settings
Publication Nutritional Content and Bioactive Compounds of Banana Peel and Its Potential Utilization: A Review(USIM Press, 2023) ;Nur Anis Insyirah Muhammad Ansari ;Nur Zazarina Ramly ;Nur Huda-FaujanNorlelawati ArifinBanana is one of the popular fruits among consumers due to their excellent nutritional value. However, banana peel, the fruit’s main secondary product or a significant by-product in banana processing, is generally abandoned and discarded as waste. Banana peels are rich in nutritional content such as protein, carbohydrates, fat, moisture, and ash contents. They are also high in bioactive compounds such as phenolic (flavonoids) and various types of carotenoids (lutein, alpha-carotene, and beta-carotene). Phenolic compounds effectively protect the human body against various diseases, specifically oxidative stress-related diseases. Due to all the advantages of banana peels, plenty of potential utilization could be explored, including citric acid production by Aspergillus niger, traditional medicine, foods, and pharmaceutical industries, as well as dietary incorporation. Thus, this paper discussed the nutritional contents and bioactive compounds of banana peel and their potential utilization as food additives, supplements, and pharmaceuticals. This could then help to minimize the number of agro-solid waste disposal from the food industry by processing the waste into value-added products. - Some of the metrics are blocked by yourconsent settings
Publication The structure of a major surface antigen SAG19 from Eimeria tenella unifies the Eimeria SAG family(Springer Nature, 2021) ;Nur Zazarina Ramly ;Samuel R. Dix ;Sergey N. Ruzheinikov ;Svetlana E. Sedelnikova ;Patrick J. Baker ;Yock-Ping Chow ;Fiona M. Tomley ;Damer P. Blake ;Kiew-Lian Wan ;Sheila NathanDavid W. RiceIn infections by apicomplexan parasites including Plasmodium, Toxoplasma gondii, and Eimeria, host interactions are mediated by proteins including families of membrane-anchored cysteine-rich surface antigens (SAGs) and SAG-related sequences (SRS). Eimeria tenella causes caecal coccidiosis in chickens and has a SAG family with over 80 members making up 1% of the proteome. We have solved the structure of a representative E. tenella SAG, EtSAG19, revealing that, despite a low level of sequence similarity, the entire Eimeria SAG family is unified by its three-layer αβα fold which is related to that of the CAP superfamily. Furthermore, sequence comparisons show that the Eimeria SAG fold is conserved in surface antigens of the human coccidial parasite Cyclospora cayetanensis but this fold is unrelated to that of the SAGs/SRS proteins expressed in other apicomplexans including Plasmodium species and the cyst-forming coccidia Toxoplasma gondii, Neospora caninum and Besnoitia besnoiti. However, despite having very different structures, Consurf analysis showed that Eimeria SAG and Toxoplasma SRS families each exhibit marked hotspots of sequence hypervariability that map to their surfaces distal to the membrane anchor. This suggests that the primary and convergent purpose of the different structures is to provide a platform onto which sequence variability can be imposed.