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Characterization of Thermostable Lactic Acid Fermenters and Enzymes (Proteases, and Chitinase) for Biowaste Valorizations and Biocontrol

Implementing Organization

Principal Investigator
Dr. Yamini Agrawal
University Of Delhi
yaminiagrawal04@gmail.com
CO-Principal Investigator
Dr. Aarti Yadav
Lady Irwin College, University Of Delhi,University Of Delhi, Sikandra Rd, Mandi House,Delhi,New Delhi-110001

Project Overview

The second most prevalent polysaccharide on our planet is chitin, which is generally found in insects, arthropods, marine animals such as shrimps and crabs, and fungi (Yan and Chen 2015; Synowiecki and Al-Khateeb 2003). An estimated 6-8 million tonnes of seafood are traded annually across the globe, consisting of lobster shells, shrimp, and crabs. These waste shells are generally disposed of in landfills or in the oceans (Basawa et al. 2023). The shells of these organisms have 15-40% of chitin, which can be used to produce valuable added products such as chitosan, chito-oligosaccharides. Further, 2000 tonnes of chitosan are produced from the leftover seafood waste from crab shells and shrimps (Santos et al. 2020). However, because of inadequate development in the technology for its processing, most of this waste is still underutilized. Traditionally, chemical processes are used leading to generation of toxic effluent, and are energy-intensive and environmentally unfriendly. In this proposal, thermostable lactic acid fermenters will facilitate demineralization, acidification of the sea food waste shells thus replacing the hazardous chemically produced acids and generation of toxic effluents. This biological acidification will create favorable condition for downstream enzymatic treatments enabling an integrated bivalorization system. Further thermostable enzymes such as proteases (EC. 3.4.21.112), are required for cleaving the residual proteins. The shells have significant proportion of residual protein which needs to be removed for extraction of high purity chitin, traditional chemical method for deproteinization involves harsh alkali treatment but thermostable proteases offer a green alternative without compromising with the enzymatic kinetics and process requirements. Thermostable chitinases (EC 3.2.1.14) will cleave the extracted chitin waste into commercially important derivatives such as chito-oligosaccharides (COS), N-acetylglucosamine. Despite their potential, there are currently limited studies towards the characterization of thermostable lactic acid fermenters, proteases and chitinases, characterizing their biochemical aspects and potential applications such as valorisation of bio waste, biological controls for pest or nematode management for commercially important crops (Telli et al. 2024). Thus, thermostable lactic acid fermenters, proteases and chitinases may be a well-suited green for bio-waste valorization and biocontrol as they are more thermally tolerant, therefore maintain the structural integrity and enzymatic activity at higher temperatures. These enzymes thus reduce the chances of contamination, operational costs, and reaction kinetics, thereby making them efficient for industrial usage. Thus, the thermostable enzymatic pathway mentioned in this proposal will be less energy-intensive, eco-friendly (Crini 2022), well aligning with the sustainable development goal SDG 9 for industrial innovation, SDG 13 climatic action and SDG 12 responsible consumption and production. The aim of the present study is to bridge this gap using a multidisciplinary approach, including molecular biology, microbiology and enzymology, to develop a commercially important green thermostable enzymes proteases & chitinases; and lactic acid producers that will have industrial as well as agricultural applications.
Funding Organization
Quick Information
Area of Research
Life Sciences & Biotechnology
Focus Area
Organismal And Evolutionary Biology (Plant Science)
Start Date
26 Mar 2026
End Date
25 Mar 2029
Status
ongoing
Output
No. of Research Paper
00
Technologies (If Any)
00
No. of PhD Produced
00
Publications
00
No. of Patents
Filed : 00
Grant : 00
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