Microbial transglutaminase-induced structural and rheological changes of cationic and anionic myofibrillar proteins

Geun Pyo Hong; Youling L. Xiong

doi:10.1016/j.meatsci.2011.12.002

Microbial transglutaminase-induced structural and rheological changes of cationic and anionic myofibrillar proteins

Geun Pyo Hong, Youling L. Xiong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

Abstract

This study investigated the effects of microbial transglutaminase (TG) on structural changes in porcine myofibrillar protein (MP) under varying pH (2.0-6.0) and two ionic strength conditions (0.1. M versus 0.6. M NaCl). Lowering the pH below the isoelectric point (pI) of myosin induced protein unfolding as revealed by surface hydrophobicity and differential scanning calorimetry. Although the MP solubility at the low ionic strength (0.1. M NaCl) was maximal at pH 3.0, both SDS-PAGE profiles and dynamic rheology indicated TG could not cross-link MP under this condition. Based on the carboxyl group content, the TG-catalyzed deamidation was dominant at a pH lower than the pI of myosin (pH 5.0) while cross-linking occurred at higher pH. Moreover, deamidation had no effect on rheological properties of MP. The results indicate that the TG reaction was governed by the pH of substrate protein, and the reaction intensity was related to the solubility of protein.

Original language	English
Pages (from-to)	36-42
Number of pages	7
Journal	Meat Science
Volume	91
Issue number	1
DOIs	https://doi.org/10.1016/j.meatsci.2011.12.002
State	Published - May 2012

Keywords

Cross-linking
Deamidation
Isoelectric point
Myofibrillar
Transglutaminase

ASJC Scopus subject areas

Food Science

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10.1016/j.meatsci.2011.12.002

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title = "Microbial transglutaminase-induced structural and rheological changes of cationic and anionic myofibrillar proteins",

abstract = "This study investigated the effects of microbial transglutaminase (TG) on structural changes in porcine myofibrillar protein (MP) under varying pH (2.0-6.0) and two ionic strength conditions (0.1. M versus 0.6. M NaCl). Lowering the pH below the isoelectric point (pI) of myosin induced protein unfolding as revealed by surface hydrophobicity and differential scanning calorimetry. Although the MP solubility at the low ionic strength (0.1. M NaCl) was maximal at pH 3.0, both SDS-PAGE profiles and dynamic rheology indicated TG could not cross-link MP under this condition. Based on the carboxyl group content, the TG-catalyzed deamidation was dominant at a pH lower than the pI of myosin (pH 5.0) while cross-linking occurred at higher pH. Moreover, deamidation had no effect on rheological properties of MP. The results indicate that the TG reaction was governed by the pH of substrate protein, and the reaction intensity was related to the solubility of protein.",

keywords = "Cross-linking, Deamidation, Isoelectric point, Myofibrillar, Transglutaminase",

author = "Hong, {Geun Pyo} and Xiong, {Youling L.}",

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language = "English",

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AU - Hong, Geun Pyo

AU - Xiong, Youling L.

PY - 2012/5

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N2 - This study investigated the effects of microbial transglutaminase (TG) on structural changes in porcine myofibrillar protein (MP) under varying pH (2.0-6.0) and two ionic strength conditions (0.1. M versus 0.6. M NaCl). Lowering the pH below the isoelectric point (pI) of myosin induced protein unfolding as revealed by surface hydrophobicity and differential scanning calorimetry. Although the MP solubility at the low ionic strength (0.1. M NaCl) was maximal at pH 3.0, both SDS-PAGE profiles and dynamic rheology indicated TG could not cross-link MP under this condition. Based on the carboxyl group content, the TG-catalyzed deamidation was dominant at a pH lower than the pI of myosin (pH 5.0) while cross-linking occurred at higher pH. Moreover, deamidation had no effect on rheological properties of MP. The results indicate that the TG reaction was governed by the pH of substrate protein, and the reaction intensity was related to the solubility of protein.

AB - This study investigated the effects of microbial transglutaminase (TG) on structural changes in porcine myofibrillar protein (MP) under varying pH (2.0-6.0) and two ionic strength conditions (0.1. M versus 0.6. M NaCl). Lowering the pH below the isoelectric point (pI) of myosin induced protein unfolding as revealed by surface hydrophobicity and differential scanning calorimetry. Although the MP solubility at the low ionic strength (0.1. M NaCl) was maximal at pH 3.0, both SDS-PAGE profiles and dynamic rheology indicated TG could not cross-link MP under this condition. Based on the carboxyl group content, the TG-catalyzed deamidation was dominant at a pH lower than the pI of myosin (pH 5.0) while cross-linking occurred at higher pH. Moreover, deamidation had no effect on rheological properties of MP. The results indicate that the TG reaction was governed by the pH of substrate protein, and the reaction intensity was related to the solubility of protein.

KW - Cross-linking

KW - Deamidation

KW - Isoelectric point

KW - Myofibrillar

KW - Transglutaminase

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JO - Meat Science

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Microbial transglutaminase-induced structural and rheological changes of cationic and anionic myofibrillar proteins

Abstract

Keywords

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