Isolation, purification, and characterization of the subtilisin inhibitor in the mung bean (Vigna radiata)
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Isolation, purification, and characterization of the subtilisin inhibitor in the mung bean (Vigna radiata)

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Published .
Written in English

Subjects:

  • Subtilisins -- Inhibitors.,
  • Mung bean.,
  • Trypsin inhibitors.

Book details:

Edition Notes

Statementby Rani Kapur.
Series[Master"s theses / University Center at Binghamton, State University of New York -- no. 1354], Master"s theses (State University of New York at Binghamton) -- no. 1354.
The Physical Object
PaginationII, 71 leaves :
Number of Pages71
ID Numbers
Open LibraryOL22180306M

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The extraction time of 2 h was optimum for the recovery of the trypsin inhibitor from mung bean seeds. The trypsin inhibitor from mung bean seeds was purified by heat-treatment at 90 °C for   The subtilisin inhibitor from double bean, cow pea and Adzuki beans were also purified employing tedious purification proce- dures [9,13,14]. It would have been ideal to use im- mobilised subtilisin for the purification of subtilisin inhibitor. However, this procedure was not adopted due to the possibility of getting modified by: 7. Isolation, Purification and Characterization of Antimicrobial Agent Antagonistic to Escherichia coli ATCC Produced by Bacillus pumilus SAFR Isolated from the Soil of Unaizah, Al Qassim Province of Saudi Arabia: Abdurrahman S. Alanazi, Kamal Ahmad Qureshi, Gamal Osman Elhassan and Elsayed I. El-Agamy. DECLARATION I hereby declare that the thesis entitled “Isolation, purification, characterization and application of proteinaceous protease inhibitor from marine bacterium Pseudomonas mendocina BTMW ” is the authentic record of research work carried out by me at the Department of Biotechnology.

the natural inhibitors of cysteine proteases (cystatins). In contrast, knowledge of inhibitors of both aspartyl and metaIloproteases IS very limited. The plant protease inhibitors differ in specificities and in their ability to inhibit one or more proteases at the same time. Majority ofthem inhibit trypsin and many inhibit chymotrypsin. Both the amino- and carboxyl-terminal residues were alaine. The inhibitor inactivated subtilisin, probably for formation of an enzyme-inhibitor complex in a molar ratio of 1: 1, but had little or no effect on the activities of other enzymes tested. The dissociation constant of the subtilisin-inhibitor complex was X 10() M. Isolation, purification and characterization of Chukwu FUNAI Journal of Science and Technology, 3(1), Page 70 relation to the dry material was calculated. The extracts obtained were stored in a refrigerator until required. Column Chromatography: A . Chapter 7 REFERENCES Abe, K., and Arai, S. (): Purification ofa cysteine proteinase inhibitor from rice, Oryza sativa1. japonica. Agri BioiC

  The lipopolysaccharide (LPS) of Vibrio cholerae O, strain CIRS, was isolated conventionally, and the lipid A was removed by mild acid hydrolysis ( m NaOAc buffer containing 1 % SDS, pH , 95 °C, 8 h). The crude product was a complex mixture consisting mainly of constituent fragments of the O‐specific polysaccharide‐core (OSPc). Abstract. The subtilisin inhibitor (MBSI-A) from the mung bean (Vigna radiata (L.) Wilczek) seed has been purified to -A consists of a single polypeptide chain of residues, with a high content of glutamic acid/glutamine, aspartic acid/asparagine, valine, threonine, and proline (19, 12, 10, 9, and 8 residue percent, respectively). I) Protein Isolation: Sources (expression) of plant proteins Heterologous expression (e.g. in bacteria, yeast or insect cells) ¾Advantages: Usually higher yield - Specific expression of one protein in large amounts and possibly with specific tag (e g His(e.g. His-tag) facilitates purificationtag) facilitates purification ¾Disadvantages. Isolation and Partial Characterization of a Subtilisin Inhibitor from the Mung Bean (Vigna radiata). Kapur R, Tan-Wilson AL, Wilson KA. Plant Physiol, 91(1), 01 Sep Cited by: 1 .