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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Main Authors: Chun-Chi Chen, Liang-Yu Chen, Der-Sheng Chan, Bang-Yuan Chen, Hsien-Wei Tseng, Jung-Feng Hsieh
Format: Article
Language:English
Published: MDPI AG 2020-09-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/25/17/3992
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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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