Effects of Mechanical Agitation, Heating and pH on the Structure of Bovine Alpha Lactalbumin
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- DHANAPATI Neupaney
- Department of Food Science, Rakuno Gakuen University
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- ISHIOROSHI Makoto
- Department of Food Science, Rakuno Gakuen University
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- YOSHIDA Ikuko
- Department of Food Science, Rakuno Gakuen University
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- SAMEJIMA Kunihiko
- Department of Food Science, Rakuno Gakuen University
Bibliographic Information
- Other Title
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- ウシαーラクトアルブミンの構造変化に及ぼす機械的撹拌加熱温度およびpHの影響
- Effects of Mechanical Agitation Heating
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Abstract
Functional properties of bovine alpha lactalbumin (α-LA) are related to its structure and are governed by changes in conformation of protein molecules. The effects of mechanical agitation, high temperature and pH on the structural changes of α-LA were examined by circular dichroism (CD), differential scanning calorimetry(DSC), spectrofluorometry, spectrophotometry, and electrical conductivity methods. The α-helixcontent decreased signifcandy below pH 5 and above pH10 The transition enthalpy values at pH2, 6.7 and 12 were 91.5, 111.6 and 100.3J/g, respectively. Heating α-L, A from 60 to 100°C at pH6.7, resulted in the increase of absorbance and electrical conductivity and the decrease in fluorescence intensity. Higher speed agitation decreased the α-helix content considerably. It is concluded that α-LA undergoes a conformational change due to strong acid and alkaline pHs, high temperatures and strong agitation.
Journal
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- Nihon Chikusan Gakkaiho
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Nihon Chikusan Gakkaiho 68 (6), 545-554, 1997
Japanese Society of Animal Science
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Keywords
Details 詳細情報について
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- CRID
- 1390282680172461056
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- NII Article ID
- 10024586747
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- NII Book ID
- AN00195188
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- ISSN
- 18808255
- 00215309
- 1346907X
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- NDL BIB ID
- 4238127
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed