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<title>Applied Sciences</title>
<link>http://dr.lib.sjp.ac.lk/handle/123456789/29</link>
<description/>
<items>
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<rdf:li rdf:resource="http://dr.lib.sjp.ac.lk/handle/123456789/13052"/>
<rdf:li rdf:resource="http://dr.lib.sjp.ac.lk/handle/123456789/12583"/>
<rdf:li rdf:resource="http://dr.lib.sjp.ac.lk/handle/123456789/12582"/>
<rdf:li rdf:resource="http://dr.lib.sjp.ac.lk/handle/123456789/12581"/>
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<dc:date>2026-04-23T15:45:52Z</dc:date>
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<item rdf:about="http://dr.lib.sjp.ac.lk/handle/123456789/13052">
<title>Proceedings of the International Forestry and Environment Symposium Volume 29 (2025)</title>
<link>http://dr.lib.sjp.ac.lk/handle/123456789/13052</link>
<description>Proceedings of the International Forestry and Environment Symposium Volume 29 (2025)
Department of Forestry and Environmental Science, University of Sri Jayewardenepura
The 29th International Forestry and Environment Symposium, is held under the theme “A Multi-Sectoral Approach to a Sustainable Future," emphasizes collaborative efforts across diverse sectors to address global challenges and achieve long-term sustainability goals. The symposium sessions delve into various aspects of this theme, presenting research findings across 12 key areas. These include Forest and Natural Resource Management, Biodiversity Conservation and Management, Waste Management and Pollution Control, Environmental Economics and Resource Management, Climate Change and Disaster Management, Biomass and Sustainable Energy, Sustainable Tourism, Sustainable Land Use and Urban Development, Wood Science and Wood Based Industries, Environmental Engineering and Green Technology, Geology, Soil and Water Resource Management, and a Citizen Science Forum. The Symposium Proceedings compile 205 abstracts of scientific studies contributed by local and international researchers.&#13;
&#13;
Online Version of Proceedings of International Forestry and Environment Symposium http://journals.sjp.ac.lk/fesympo
</description>
<dc:date>2025-01-17T00:00:00Z</dc:date>
</item>
<item rdf:about="http://dr.lib.sjp.ac.lk/handle/123456789/12583">
<title>Functional and antiglycation properties of cow milk set yogurt enriched with Nyctanthes arbor-tristis L. fower extract</title>
<link>http://dr.lib.sjp.ac.lk/handle/123456789/12583</link>
<description>Functional and antiglycation properties of cow milk set yogurt enriched with Nyctanthes arbor-tristis L. fower extract
Amadarshanie, D.B.T.; Gunathilaka, T.L.; Silva, R.M.; Navaratne, S.B.; Peiris, L.D.C.
The fortifcation of yogurt with natural herbs to improve its nutritional and health beneft are an emerging trend.&#13;
Hot infusions of Nyctanthes abo-tristis fowers are a traditionally used herb against diabetes. This study was&#13;
designed to develop a novel yogurt fortifed (FY) with 3, 3.5, and 6% N.arbor-tristis fower extract (NFE) to&#13;
determine its suitability as a fortifer en route to innovative functional products. Upon fermentation, the highest&#13;
sensory scores were obtained for the 3.5% NFE-FY with 11-, 6-, 3-fold higher antiglycation (NFE- IC50: 28.04 ±&#13;
1.13 μg/mL and 3.5% NFE-FY IC50: 46.80 ± 0.92 μg/mL) activity, free radical scavenging potentials, and total&#13;
phenolic content, respectively. An improvement of texture profle values was observed in 3.5% NFE-FY compared&#13;
to the control with 3.00 ± 0.1% fat, 3.88 ± 0.23% crude protein, 77.94 ± 0.09 moisture, 14.97 ± 0.27 total&#13;
soluble solids, and 0.7637 ± 0.03 ash. The 3.5%NEF-FY also exhibited a longer shelf life and less microbial&#13;
growth than the control. The GC-MS analysis of the NFE indicated the presence of phytochemicals essential for&#13;
the observed bioactivity. The results confrmed that the N.arbor-tristis fower extract increased the overall quality&#13;
of the yogurt and tested bioactivity. NFE-FY could be used in yogurt production to optimize the health benefts&#13;
with improved functional characteristics to prevent diet-driven glycation activity.
</description>
<dc:date>2022-01-01T00:00:00Z</dc:date>
</item>
<item rdf:about="http://dr.lib.sjp.ac.lk/handle/123456789/12582">
<title>Integration of in vitro and in‑silico analysis of Caulerpa racemosa against antioxidant, antidiabetic, and anticancer activities</title>
<link>http://dr.lib.sjp.ac.lk/handle/123456789/12582</link>
<description>Integration of in vitro and in‑silico analysis of Caulerpa racemosa against antioxidant, antidiabetic, and anticancer activities
Dissanayake, I.H.; Bandaranayake, U.; . Keerthirathna, L.R.; Manawadu, C.; Silva, R.M.; Mohamed, B.; Rizwan, A.; Peiris, D.C.
Marine algae are found to be excellent in their nutritional and potential therapeutic properties.&#13;
This study explores the antidiabetic and anticancer potential of fractionated polyphenolic extract&#13;
of Caulerpa racemosa, green macroalgae. Crude polyphenolic extract (CPE) of C. racemosa and its&#13;
fractions (n-hexane, ethyl acetate, chloroform, and distilled water) were tested for its total phenol&#13;
and favonoid contents and antioxidant potential. The ethyl acetate fraction was subjected to gas&#13;
chromatography/mass spectrometry (GC/MS). The in vitro antidiabetic activity was assessed by alphaamylase, glucosidase inhibition and anti-glycation assays. Also, in-silico studies were conducted to&#13;
test the binding afnities between caulerpin with alpha-glucosidase enzyme and estrogen receptor&#13;
(ER) active sites. Each fraction was tested for its in vitroin vitroanticancer activity by CellTiter-Glo and&#13;
MTT cell proliferation assays. The total phenolic and favonoid contents and the antioxidant potential&#13;
of the crude extract were observed to be dose dependent. The GC/MS analysis of the ethyl acetate&#13;
fraction yielded 47 peaks, whereas n-hexadecanoic acid and hexadecanoic acid methyl ester showed&#13;
the highest compatibility percentages of 99% and 96%, respectively. The CPE exhibited a higher&#13;
potential in both alpha-amylase inhibitory and anti-glycation activities. The ethyl acetate fraction&#13;
was more efective against alpha-glucosidase inhibition. Molecular docking revealed a high binding&#13;
afnity between the alpha-glucosidase enzyme and caulerpin and showed high binding afnity toward&#13;
caulerpin, with H-bond interactions. The in vitro anticancer analyses revealed that chloroform fraction&#13;
and CPE exhibited moderate activity on the KAIMRC1 cell line. Also, the CPE exhibited high specifcity&#13;
compared to the standard drug in anticancer studies. Our fndings evidence the pharmacological&#13;
potential of the CPE of C. racemosa, and bioactive compounds of the species may be utilized as lead&#13;
molecules to develop anti-diabetic and anti-cancer drugs.
</description>
<dc:date>2022-01-01T00:00:00Z</dc:date>
</item>
<item rdf:about="http://dr.lib.sjp.ac.lk/handle/123456789/12581">
<title>In silico study of SARS‐CoV‐2 spike protein RBD and human ACE‐2 affinity dynamics across variants and Omicron subvariants</title>
<link>http://dr.lib.sjp.ac.lk/handle/123456789/12581</link>
<description>In silico study of SARS‐CoV‐2 spike protein RBD and human ACE‐2 affinity dynamics across variants and Omicron subvariants
Abeywardhana, S.; Premathilaka, M.; Bandaranayake, U.; Perera, D.; Peiris, L.D.C.
The coronavirus disease 2019 virus outbreak continues worldwide, with many&#13;
variants emerging, some of which are considered variants of concern (VOCs). The&#13;
WHO designated Omicron as a VOC and assigned it under variant B.1.1.529. Here,&#13;
we used computational studies to examine the VOCs, including Omicron&#13;
subvariants, and one variant of interest. Here we found that the binding affinity&#13;
of human receptor angiotensin‐converting enzyme 2 (hACE2) and receptor‐binding&#13;
domain (RBDs) increased in the order of wild type (Wuhan‐strain) &lt; Beta&#13;
&lt; Alpha &lt; OmicronBA.5 &lt; Gamma &lt; Delta &lt; Omicron BA.2.75 &lt; BA.1 &lt; BA.3 &lt; BA.2.&#13;
Interactions between docked complexes revealed that the RBD residue positions&#13;
like 452, 478, 493, 498, 501, and 505 are crucial in creating strong interactions&#13;
with hACE2. Omicron BA.2 shows the highest binding capacity to the hACE2&#13;
receptor among all the mutant complexes. The BA.5's L452R, F486V, and T478K&#13;
mutation significantly impact the interaction network in the BA.5 RBD‐hACE2&#13;
interface. Here for the first time, we report the His505, an active residue on the&#13;
RBD forming a salt bridge in the BA.2, leading to increased mutation stability.&#13;
When the active RBD residues are mutated, binding affinity and intermolecular&#13;
interactions increase across all mutant complexes. By examining the differences in&#13;
different variants, this study may provide a solid foundation for structure‐based&#13;
drug design for newly emerging variants.
</description>
<dc:date>2022-01-01T00:00:00Z</dc:date>
</item>
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