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Title: | Multi-component thermostable cellulolytic enzyme production by Aspergillus niger HN-1 using pea pod waste: Appraisal of hydrolytic potential with lignocellulosic biomass. |
Other Titles: | Not Available |
Authors: | Reetika Sharma, Rekha Rawat, Ravinder Singh Bhogal and Harinder Singh Oberoi |
ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
Author's Affiliated institute: | ICAR::Indian Institute of Horticultural Research ICAR-Central Institute of Post Harvest Engineering and Technology |
Published/ Complete Date: | 2015-02-12 |
Project Code: | Not Available |
Keywords: | Aspergillus niger HN-1;Cellulolytic enzymes; Hydrolysis; Pea pod waste; Response surface methodology; Sweet sorghum bagasse |
Publisher: | Elsevier |
Citation: | Not Available |
Series/Report no.: | Not Available; |
Abstract/Description: | Solid state fermentation with pea pod waste and Aspergillus niger HN-1 resulted in filter paper cellu-lase (FP) and -glucosidase (BGL) activity of 30 FPU/gds and 270 U/gds, respectively. Validation withthe response surface optimized parameters (moisture content: 65%, pH 6.0, temperature: 33◦C, time:84 h) in a solid-state tray fermentation enhanced FP and BGL activity by about 40 and 28%, respectively.Multi-component enzyme from A. niger HN-1 produced FP, BGL, endoglucanase (EG), cellobiohy-drolase (CBHI), xylanase, -l-arabinofuranosidase, -xylosidase and xylan esterase with activities of41.07 ± 2.11 FPU/gds, 345.69 ± 17.1, 480.3 ± 21.5, 52.1 ± 1.5, 2800.5 ± 88.4, 88.1 ± 9.3, 280.8 ± 11.4 and3321.7 ± 14.8 U/gds, respectively. Enzyme was optimally active at temperature and pH of 55◦C and 5.0,respectively and demonstrated thermostability by retaining >95% activity for 6 h at 55◦C. SDS-PAGEshowed the presence of 11 protein bands with molecular mass ranging between 20 and 200 kDa, whilezymogram revealed the presence of multiple forms of EG, CBH and BGL with varying molecular mass.Hydrolysis of sweet sorghum bagasse at relatively high substrate loading (15%, w/v) with crude enzymeat 20 FPU/gds in thermostatically controlled glass reactor led to conversion of 82–91% of holocellulose tofermentable sugars in just 24 h as evident from HPLC analysis, showing promise for the reported enzymein bioprocessing applications. |
Description: | Not Available |
Type(s) of content: | Research Paper |
Sponsors: | AMAAS sub-project (NBAIM/AMAAS/2008-09/AMBPH-05/HSO/BG/3/5982) from the Indian Council of Agricul-tural Research (ICAR), Government of India. |
Language: | English |
Name of Journal: | Process Biochemistry |
Volume No.: | 50 |
Page Number: | 696-704 |
Name of the Division/Regional Station: | Post Harvest Technology and Agricultural Engineering |
Source, DOI or any other URL: | http://dx.doi.org/10.1016/j.procbio.2015.01.025 |
URI: | http://krishi.icar.gov.in/jspui/handle/123456789/23504 |
Appears in Collections: | HS-IIHR-Publication |
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