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Chaudhary Charan Singh Haryana Agricultural University, Hisar

Chaudhary Charan Singh Haryana Agricultural University popularly known as HAU, is one of Asia's biggest agricultural universities, located at Hisar in the Indian state of Haryana. It is named after India's seventh Prime Minister, Chaudhary Charan Singh. It is a leader in agricultural research in India and contributed significantly to Green Revolution and White Revolution in India in the 1960s and 70s. It has a very large campus and has several research centres throughout the state. It won the Indian Council of Agricultural Research's Award for the Best Institute in 1997. HAU was initially a campus of Punjab Agricultural University, Ludhiana. After the formation of Haryana in 1966, it became an autonomous institution on February 2, 1970 through a Presidential Ordinance, later ratified as Haryana and Punjab Agricultural Universities Act, 1970, passed by the Lok Sabha on March 29, 1970. A. L. Fletcher, the first Vice-Chancellor of the university, was instrumental in its initial growth.

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2013 - 20172
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Subject: Microbiology × Author: Bhatia, Tanvi × End date: 2019 × Type: Thesis ×
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    ThesisItemOpen Access
    Evaluation of ligninolytic and cellulolytic fungi for degradation of lignocellulosic wastes
    (CCSHAU, 2017) Bhatia, Tanvi; Goyal, Sneh
    Fungi play an important role in the biodegradation of lignocellulosic substrates. Therefore, the uses of lignocellulolytic fungi for biotechnological applications are quite promising. In present investigation, 43 mutually distinct fungi were isolated from different samples and screened for their ligninolytic and cellulolytic activities. Physical conditions for nine promising isolates SMT1, SMT2, SMT22, SMT29, HST9, HST11, HST14, HST15 and HST16 were optimized for production of lignocellulose degrading enzymes; laccase, lignin peroxidase, manganese peroxidase, carboxy methyl cellulase and filter paper degrading activities.All the isolates showed maximum enzyme activities at 30OC temperature, pH 6, on 6th day of incubation and under stationary conditions.Maximum cellulolytic activities were shown bySMT2followed by SMT1 and maximum ligninolytic activities were shown by SMT22 followed by SMT29. Laccase, LiP and MnP activities decreased after addition of metal ions; however, cellulase activities remained unaffected in the presence of metal ions at optimum concentration.Among different cellulose substrates, carboxymethyl cellulose (200 mg/L) concentration was optimized which gave maximum FPase and CMCase activities in case of isolate SMT2. The isolate SMT29 gave maximum laccase activity and SMT22 showed maximum lignin peroxidase and manganese peroxidase activities at 100 mg/L concentration of alkali lignin.The addition of different ammonium salts at (0.5g/L) showed highest FPase activity in SMT1 in case of ammonium sulfate whereas highest CMCase activity by SMT2 was observed for ammonium chloride. Maximum laccase activity was given by SMT22 in case of ammonium chloride whereas maximum lignin peroxidase activity was given by SMT29 after addition of ammonium sulfate.In case of corn cob, maximum loss in TOM was observed for SMT22 (65.57%)followed by SMT29 (64.67%); however, in case of sugarcane bagasse, maximum loss in TOM was observed for SMT29 (33.75%) followed by SMT22 (33.68%). Initial cellulose, hemicellulose and lignin concentration in corn cob were 35, 42 and 14% respectively, which reduced to 17, 31 and 9% respectively, in case of SMT2 and 18, 21 and 1% respectively, in case of SMT22 after 30 days of incubation. Likewise, initial concentration of cellulose, hemicellulose and lignin were 41, 25 and 20% in sugarcane bagasse respectively, which reduced to 31, 15 and 4% respectively, in case of SMT22 and 28, 17 and 13% respectively, in case of SMT2 after 30 days of incubation.On the basis of microscopic characteristics, 7 fungal isolates were identified to be ascomycetes and 2 were basidiomycetes and on the basis of molecular characterization, SMT2 was identified to be Alternariatenuissima, SMT22 was identified as Aspergillusterreus strain FJAT-31011 and HST9 was identified as Aspergillusdentatus (Emericella dentate).
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    ThesisItemOpen Access
    Isolation and screening of efficient ligninolytic fungi
    (CCSHAU, 2013) Bhatia, Tanvi; Goyal, Sneh
    Lignin, the most abundant aromatic biopolymer on earth, is extremely recalcitrant to degradation. By linking to both cellulose and hemicellulose, it creates a barrier to any chemicals or enzymes and prevents the penetration of lignocellulolytic enz ymes into the interior lingocellulosic structure. Lignin is the major hurdle in the degradation of lignocellulosic biomass. It is degraded by an enzyme complex containing three enzymes namely laccase, manganese peroxidase and lignin peroxidase that are collectively known as ligninases. These enzymes are produced by several microorganisms, commonly by fungi but most of them have high production cost and no efficiency in enzyme production and its enzyme activit y. Therefore in the present investigation, a total of 24 mutually distinct fungi were isolated from different ecological niches such as leaf and litter waste, garbage dumpin g site, mushr oom waste, compost, ver micompost, paper and pulp waste and biogas slurry. Out of these 24 fungal isolates, 16 fungal cultures were screened as ligninolytic fungi by observing the formation of zone of clearance on malt extract agar plates containing aniline blue dye and tannic acid. The zone of clearance ranged from 1.03 to 1.20 Isolate HST15 formed the largest zone of clearance of 1.20. The fungal isolate, HST9 was showing highest laccase (15.5 U/ml) and Manganese peroxidase (4 U/ml) activity among the isolates while maximum lignin peroxidase activity was observed in HST15 (21U/ml). On the basis of lignin peroxidase activity, HST15 was selected as the best ligninolytic fungal isolate. The selected fungal isolates were morphologically identified on the basis of their hyphae, sporangiophore and spores. Among the five best fungal isolates, three were identified to be ascomycetes and two were basidiomycetes.