Effect of acetylation on functionality of soybean glycinin = 아세틸화에 의한 콩의 Glycinin의 기능성 변화

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Acetylation of $\varepsilon$-amino groups of lysines changed the conformation of glycinin isolated from soybean. Soy glycinin with lysine residues modifications of 0\%, 25\%, 65\% and 95\% were used for the experiment. Surface hydrophobicity was found to increase in about 3 times when lysine residues were excessively modified to above 95\%. Masking of charged lysine residues, exposure of hydrophobic interior and subunit dissociation should have contributed to the conformational change that can be detected by UV spectra and the change of the intensity of effectiveness of pH, salts, temperature and conglycinin aggregation or solubilization of glycinin. The effect of acetylation on solubility of protein was investigated. Solubility of glycinin was increased and isoelectric point was shifted to acidic region. Salts (NaCl, CaCl$_2$) were found to little affect solubility of acetylated glycinin in contrast to native one. Heat stability of acetylated glycinin was increased, conglycinin affected little on solubility of acetylated glycinin in contrast to native one.
Advisors
Rhee, Joon-Shick이준식
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1989
Identifier
66643/325007 / 000871068
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1989.2, [ v, 48 p. ]

Keywords

단백질 화학 변형.

URI
http://hdl.handle.net/10203/28306
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=66643&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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