Effects of sodium hexametaphosphate, sodium tripolyphosphate and sodium pyrophosphate on the ultrastructure of beef myofibrillar proteins investigated with atomic force microscopy

Yunpeng Hu; Lan Zhang; Yuwen Yi; Iftikhar Solangi; Linsen Zan; Jie Zhu

doi:10.1016/j.foodchem.2020.128146

Effects of sodium hexametaphosphate, sodium tripolyphosphate and sodium pyrophosphate on the ultrastructure of beef myofibrillar proteins investigated with atomic force microscopy

Food Chem. 2021 Feb 15:338:128146. doi: 10.1016/j.foodchem.2020.128146. Epub 2020 Sep 21.

Authors

Yunpeng Hu¹, Lan Zhang¹, Yuwen Yi², Iftikhar Solangi¹, Linsen Zan³, Jie Zhu⁴

Affiliations

¹ Laboratory of Agricultural and Food Biomechanics, Institute of Biophysics and College of Science, Northwest A&F University, Yangling, Shaanxi 712100, China.
² Sichuan Key Laboratory of Cooking Science, Sichuan Tourism University, Chengdu, Sichuan 610100, China.
³ Laboratory of Muscle & Meat Biomechanics, National Beef Cattle Improvement Center, Northwest A&F University, Yangling, Shaanxi 712100, China; Laboratory of Meat Quality Analysis and Products Development, Ningxia Xihaigu Institute of Premium Cattle Industry, Haiyuan, Ningxia 755299, China.
⁴ Laboratory of Agricultural and Food Biomechanics, Institute of Biophysics and College of Science, Northwest A&F University, Yangling, Shaanxi 712100, China; Laboratory of Muscle & Meat Biomechanics, National Beef Cattle Improvement Center, Northwest A&F University, Yangling, Shaanxi 712100, China; Laboratory of Meat Quality Analysis and Products Development, Ningxia Xihaigu Institute of Premium Cattle Industry, Haiyuan, Ningxia 755299, China. Electronic address: [email protected].

PMID: 33091990
DOI: 10.1016/j.foodchem.2020.128146

Abstract

Myofibrillar protein isolated from beef muscles were treated with 3 phosphates (Sodium Hexametaphosphate, sodium tripolyphosphate, sodium pyrophosphate) with different concentrations of 0.3%, 0.6%, 0.9%, 1.2% respectively. Protein solubility, surface hydrophobicity and reactive sulfhydryl group was determined. Atomic force microscopy was used to observe the microscopic protein surface. SDS-PAGE was carried out to determine the proteolysis of myofibrillar protein. The solubility and surface hydrophobic bond of myofibrillar protein was highly increased and the diameter decreased by SHMP, TSPP, STPP. Reactive sulfhydryl groups increased after SHMP addition, but slightly decreased in STPP and TSPP treated MP. TSPP and STPP had the same effect on myofibrillar microstructure and was different from SHMP. Three phosphates all caused MP unfolding. The MP gel complexity was increased, and roughness was decreased after phosphates addition, indicating phosphates helped to construct a more ordered and smoother gel microcosmic surface.

Keywords: Atomic force microscopy; Myofibrillar proteins; Sodium Tripolyphosphate; Sodium hexametaphosphate; Sodium pyrophosphate; Ultrastructure.

MeSH terms

Animals
Cattle
Diphosphates / chemistry*
Hydrophobic and Hydrophilic Interactions
Microscopy, Atomic Force*
Muscle Proteins / chemistry*
Phosphates / chemistry*
Polyphosphates / chemistry*
Red Meat*
Solubility

Substances

Diphosphates
Muscle Proteins
Phosphates
Polyphosphates
triphosphoric acid
sodium pyrophosphate
sodium polymetaphosphate