Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins
The effects of microbial transglutaminase (MTGase) cross-linking on the physicochemical characteristics of individual caseins were investigated. MTGase was used to modify three major individual caseins, namely, κ-casein (κ-CN), α<sub>S</sub>-casein (α<sub>S</sub>-CN) and β-ca...
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2020-09-01
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author | Chun-Chi Chen Liang-Yu Chen Der-Sheng Chan Bang-Yuan Chen Hsien-Wei Tseng Jung-Feng Hsieh |
author_facet | Chun-Chi Chen Liang-Yu Chen Der-Sheng Chan Bang-Yuan Chen Hsien-Wei Tseng Jung-Feng Hsieh |
author_sort | Chun-Chi Chen |
collection | DOAJ |
description | The effects of microbial transglutaminase (MTGase) cross-linking on the physicochemical characteristics of individual caseins were investigated. MTGase was used to modify three major individual caseins, namely, κ-casein (κ-CN), α<sub>S</sub>-casein (α<sub>S</sub>-CN) and β-casein (β-CN). The SDS-PAGE analysis revealed that MTGase-induced cross-linking occurred during the reaction and that some components with high molecular weights (>130 kDa) were formed from the individual proteins κ-CN, α<sub>S</sub>-CN and β-CN. Scanning electron microscopy (SEM) and particle size analysis respectively demonstrated that the κ-CN, α<sub>S</sub>-CN and β-CN particle diameters and protein microstructures were larger and polymerized after MTGase cross-linking. The polymerized κ-CN (~749.9 nm) was smaller than that of β-CN (~7909.3 nm) and α<sub>S</sub>-CN (~7909.3 nm). The enzyme kinetics results showed <i>K</i><sub>M</sub> values of 3.04 × 10<sup>−6</sup>, 2.37 × 10<sup>−4</sup> and 8.90 × 10<sup>−3</sup> M for κ-CN, α<sub>S</sub>-CN and β-CN, respectively, and, furthermore, <i>k</i><sub>cat</sub> values of 5.17 × 10<sup>−4</sup>, 1.92 × 10<sup>−3</sup> and 4.76 × 10<sup>−2</sup> 1/s, for κ-CN, α<sub>S</sub>-CN and β-CN, respectively. Our results revealed that the cross-linking of β-CN catalyzed by MTGase was faster than that of α<sub>S</sub>-CN or κ-CN. Overall, the polymers that formed in the individual caseins in the presence of MTGase presented a higher molecular weight and larger particles. |
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spelling | doaj.art-0f88d131006b406abef63ca9c536e5632023-11-20T12:14:36ZengMDPI AGMolecules1420-30492020-09-012517399210.3390/molecules25173992Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual CaseinsChun-Chi Chen0Liang-Yu Chen1Der-Sheng Chan2Bang-Yuan Chen3Hsien-Wei Tseng4Jung-Feng Hsieh5Department of Biological Science and Technology, School of Life Sciences, Longyan University, Longyan 364012, ChinaDepartment of Food Science, Fu Jen Catholic University, New Taipei City 242, TaiwanDepartment of Information Technology, Lee-Ming Institute of Technology, New Taipei City 243, TaiwanDepartment of Food Science, Fu Jen Catholic University, New Taipei City 242, TaiwanDepartment of Mathematics and Information Engineering, Longyan University, Longyan 364012, ChinaDepartment of Food Science, Fu Jen Catholic University, New Taipei City 242, TaiwanThe effects of microbial transglutaminase (MTGase) cross-linking on the physicochemical characteristics of individual caseins were investigated. MTGase was used to modify three major individual caseins, namely, κ-casein (κ-CN), α<sub>S</sub>-casein (α<sub>S</sub>-CN) and β-casein (β-CN). The SDS-PAGE analysis revealed that MTGase-induced cross-linking occurred during the reaction and that some components with high molecular weights (>130 kDa) were formed from the individual proteins κ-CN, α<sub>S</sub>-CN and β-CN. Scanning electron microscopy (SEM) and particle size analysis respectively demonstrated that the κ-CN, α<sub>S</sub>-CN and β-CN particle diameters and protein microstructures were larger and polymerized after MTGase cross-linking. The polymerized κ-CN (~749.9 nm) was smaller than that of β-CN (~7909.3 nm) and α<sub>S</sub>-CN (~7909.3 nm). The enzyme kinetics results showed <i>K</i><sub>M</sub> values of 3.04 × 10<sup>−6</sup>, 2.37 × 10<sup>−4</sup> and 8.90 × 10<sup>−3</sup> M for κ-CN, α<sub>S</sub>-CN and β-CN, respectively, and, furthermore, <i>k</i><sub>cat</sub> values of 5.17 × 10<sup>−4</sup>, 1.92 × 10<sup>−3</sup> and 4.76 × 10<sup>−2</sup> 1/s, for κ-CN, α<sub>S</sub>-CN and β-CN, respectively. Our results revealed that the cross-linking of β-CN catalyzed by MTGase was faster than that of α<sub>S</sub>-CN or κ-CN. Overall, the polymers that formed in the individual caseins in the presence of MTGase presented a higher molecular weight and larger particles.https://www.mdpi.com/1420-3049/25/17/3992transglutaminaseκ-caseinα<sub>S</sub>-caseinβ-caseincross-linking |
spellingShingle | Chun-Chi Chen Liang-Yu Chen Der-Sheng Chan Bang-Yuan Chen Hsien-Wei Tseng Jung-Feng Hsieh Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins Molecules transglutaminase κ-casein α<sub>S</sub>-casein β-casein cross-linking |
title | Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins |
title_full | Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins |
title_fullStr | Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins |
title_full_unstemmed | Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins |
title_short | Influence of Microbial Transglutaminase on Physicochemical and Cross-Linking Characteristics of Individual Caseins |
title_sort | influence of microbial transglutaminase on physicochemical and cross linking characteristics of individual caseins |
topic | transglutaminase κ-casein α<sub>S</sub>-casein β-casein cross-linking |
url | https://www.mdpi.com/1420-3049/25/17/3992 |
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