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2014 | 09 |

Tytuł artykułu

Optimization and production of alkaline proteases from agro byproducts using a novel Trichoderma viridiae strain VPG 12, isolated from agro soil

Treść / Zawartość

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
In recent years, there has been a phenomenal increase in the use of alkaline proteases as industrial catalysts. The aim of this work was to isolate potent fungal strain from the agricultural field of Gulbarga region of India, for the production of alkaline protease by utilizing the agricultural by products viz, red and green gram and Bengal gram as substrate under submerged fermentation process. Optimization of fermentation process parameters such as substrate (Red gram husk, green gram husk and Bengal gram husk) utilization, utilization, temperature, pH and incubation period for alkaline protease production was carried out. The maximum production of alkaline protease by Trichoderma VPG 12 was found at pH 8, temperature 35 °C, incubated for 120 h. But the activity of the enzyme could also be seen in a wide range of pH (5-9) and temperature (20-40 °C). With all these properties, the strain can be considered for industrial grade production of alkaline protease.

Wydawca

-

Rocznik

Tom

09

Opis fizyczny

p.77-84,fig.,ref.

Twórcy

  • Department of Biotechnology, Gulbarga University, Gulbarga - 585106, Karnataka, India
  • Department of Biotechnology, Gulbarga University, Gulbarga - 585106, Karnataka, India
  • Department of Botany, Sikkim Central University, Gangtok - 737102, Sikkim, India
autor
  • Centre for Studies in Biotechnology, Dibrugarh University, Dibrugarh - 786004, India
  • Department of Biotechnology, GITAM Institute of Science, GITAM University, Vishakhapatnam - 530045, India

Bibliografia

  • [1] Ashokan P., Mohini S., Shyam R. A., Building and Environment 42 (2007) 2311-2320.
  • [2] Sumantha A., Larroche C., Ashok P., Food Technol. Biotechnol 44 (2) (2006) 211-220.
  • [3] Godfrey T., Leather in Industrial Enzymology 2 (1996) 285-291.
  • [4] McDonald C. E., Chen L. L., Analytical Biochemistry 10(1) (1965) 175-177. [5] Ellaiah P., Srinivasulu B., Adinarayana K., J Sci Indstr Res 61 (2002) 690-704.
  • [6] Gupta R., Beg Q. K., Khan S., Chauhan B., Appl Microbiol Biotech 60 (2002) 381-395.
  • [7] Kalpana Devi M., Rasheedha B. A., Gnanaprabhal G. R., Pradeep B.V., Palaniswamy M., Ind J Science Tech 1(7) (2008) 1-6.
  • [8] Rao M. B., Tanksale A. M., Ghatge M. S., Deshpande V. V., Microbiol Mol Biol Rev 62 (1998) 597-635.
  • [9] Nakayama M., Tomita Y., Suzuki H., Nisizawa K., J Biochem 79 (1976) 955-966.
  • [10] Jeswani L. M., Baldev B., Adv in Pulse Pro Tech, Indian Council of Agricultural Research Publication (1988).
  • [11] Uchikoba T., Mase T., Arima K., Yonezawa H., Kaneda M., Biol Chem 382 (2001) 1509-1513.
  • [12] Manczinger L., Antal Z., Schoop A., Kredics L., Acta Biol Hung 52 (2001) 223-229.
  • [13] Lowry O. H., Rosebrough N., Farr A. L., Ronadall R. L., J. Biol. Chem 193 (1951) 265-273.
  • [14] Nehra K. S., Dhilon S., Chaudhary K., Singh R., Ind. J. Microbial. 42 (2002) 43-47.
  • [15] Joo H. S., Ganeshkumar C., Park G. C., Kim K. T., Seung R., Paik Chang C. S., Process Biochem 38 (2002) 155-159.
  • [16] Gessesse A., Bioresour. Technol 62 (1997) 56- 61.
  • [17] Zwietering M. H., Jongenburger I., Rombouts F. M., Van't Riet K., Applied and Environmental Microbiology 56 (1990) 1875-1881.
  • [18] Malherbe S., Fromion V., Hilgert N., Sablayrolles J. M., Biotechnology and Bioengineering 86 (2004) 261–272.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-21f39aad-bd62-4b5c-8b4d-b989f39fcf76
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