Study on the Structure and Functional Characteristics of Proteins from Haematococcus pluvialis
Haematococcus pluvialis residue powder, which has been extracted with astaxanthin, was used as the raw material to prepare Haematococcus pluvialis protein by alkaline extraction and acid precipitation method. The protein structure of Haematococcus pluvialis was characterized, and the effects of pH a...
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Published in | Liang you shipin ke-ji Vol. 32; no. 4; pp. 201 - 209 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Academy of National Food and Strategic Reserves Administration
01.07.2024
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Subjects | |
Online Access | Get full text |
ISSN | 1007-7561 |
DOI | 10.16210/j.cnki.1007-7561.2024.04.025 |
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Abstract | Haematococcus pluvialis residue powder, which has been extracted with astaxanthin, was used as the raw material to prepare Haematococcus pluvialis protein by alkaline extraction and acid precipitation method. The protein structure of Haematococcus pluvialis was characterized, and the effects of pH and ion strength on the functional characteristics of Haematococcus pluvialis protein were studied. The results showed that the isoelectric point of Haematococcus pluvialis protein was 4.2. The molecular weight of the subunit was around 14.4, 18.4 and 38 kDa, respectively and the content of α-helix, β-fold, β-corner and disordered structure in the secondary structure was 14.86%, 18.47%, 40.3% and 26.37%, respectively. It contained 7 kinds of essential amino acids required by the human body, accounting for 36.38% of the total amino acid content. Microscopic observation showed that the protein of Haematococcus pluvialis was rod-shaped and sheet-like, with a rough and porous surface. With the increase of pH, the solubility, water absorption, emulsion capability, foam stability and foam stability of the protein of Haematococcus pluvialis increased first and then decreased, while the emulsification stability showed the opposite trend. With the increase of NaCl concentration, the foam capability, foam stability, emulsion capability and emulsification stability of the protein of Haematococcus pluvialis increased first and then decreased, while the solubility showed a trend of first decreasing, then increasing, and then decreasing again. |
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AbstractList | Haematococcus pluvialis residue powder, which has been extracted with astaxanthin, was used as the raw material to prepare Haematococcus pluvialis protein by alkaline extraction and acid precipitation method. The protein structure of Haematococcus pluvialis was characterized, and the effects of pH and ion strength on the functional characteristics of Haematococcus pluvialis protein were studied. The results showed that the isoelectric point of Haematococcus pluvialis protein was 4.2. The molecular weight of the subunit was around 14.4, 18.4 and 38 kDa, respectively and the content of α-helix, β-fold, β-corner and disordered structure in the secondary structure was 14.86%, 18.47%, 40.3% and 26.37%, respectively. It contained 7 kinds of essential amino acids required by the human body, accounting for 36.38% of the total amino acid content. Microscopic observation showed that the protein of Haematococcus pluvialis was rod-shaped and sheet-like, with a rough and porous surface. With the increase of pH, the solubility, water absorption, emulsion capability, foam stability and foam stability of the protein of Haematococcus pluvialis increased first and then decreased, while the emulsification stability showed the opposite trend. With the increase of NaCl concentration, the foam capability, foam stability, emulsion capability and emulsification stability of the protein of Haematococcus pluvialis increased first and then decreased, while the solubility showed a trend of first decreasing, then increasing, and then decreasing again. |
Author | YUAN Shuo ZHAO Xiao-yan LI Qin ZHANG Xiao-wei ZHU Yun-ping WANG Meng LIU Hong-kai |
Author_xml | – sequence: 1 fullname: LI Qin organization: School of Biological Science and Technology, University of Jinan, Jinan, Shandong 250022, China; School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 2 fullname: WANG Meng organization: School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 3 fullname: YUAN Shuo organization: School of Biological Science and Technology, University of Jinan, Jinan, Shandong 250022, China; School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 4 fullname: ZHAO Xiao-yan organization: School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 5 fullname: LIU Hong-kai organization: School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 6 fullname: ZHANG Xiao-wei organization: School of Culinary, University of Jinan, Jinan, Shandong 250022, China – sequence: 7 fullname: ZHU Yun-ping organization: School of Food and Health, Beijing Technology and Business University, Beijing 100048, China |
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Title | Study on the Structure and Functional Characteristics of Proteins from Haematococcus pluvialis |
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