Recombinant metalloprotease as a perspective enzyme for meat tenderization

Minaev, M. Yu.; Makhova, A.A.

doi:10.5219/1087

Cited by 4 publications

(2 citation statements)

References 19 publications

(6 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, we previously obtained the recombinant metallopeptidase from Aeromonas salmonicida using the transformation of Pichia pastoris for subsequent softening of meat. Histological examination of beef shank samples found a pronounced separation of the perimeter from the muscle bundles and the breakdown of collagen fibers, while the muscle fibers remained unchanged [54].…”

Section: Enzymes Of Fungal and Bacterial Originmentioning

confidence: 97%

“…Industrial use of microbial collagenases is limited by safety concerns related to their potential toxicity and the other adverse effects [78]. One of possible approaches involves the production of recombinant collagenases [54] in non-pathogenic microorganisms to avoid contamination by associated virulence factors. For example, we previously obtained the recombinant metallopeptidase from Aeromonas salmonicida using the transformation of Pichia pastoris for subsequent softening of meat.…”

Section: Enzymes Of Fungal and Bacterial Originmentioning

confidence: 99%

See 1 more Smart Citation

The role of enzymes in the formation of meat and meat products

Khvostov,

Khryachkova,

Minaev

2024

Teor. prakt. pererab. mâsa (Print)

Self Cite

View full text Add to dashboard Cite

The meat industry is one of the most dynamic and competitive sectors of the food industry. As the global population keeps on growing and the demand for protein does the same, the consumers define ever higher standards of quality for the meat producers. One of the key quality criteria is the tenderness and juiciness of meat, which directly affects its taste and texture characteristics. In order to satisfy the expectations of the modern consumers and to ensure the stable quality of the meat product, meat processing enterprises actively introduce the innovative technologies. In recent decades, proteolytic enzymes have been increasingly used to improve the quality characteristics of the meat products, which is a more progressive method in comparison with to mechanical methods of processing due to less impact on other consumer properties. This article overviews the role and importance of enzymes in the meat industry. We will consider various aspects of the application of these enzymes for the meat products, their effect on the level of tenderness, juiciness and other characteristics of meat, as well as prospects for the further development of their using

show abstract

Section: Enzymes Of Fungal and Bacterial Originmentioning

confidence: 97%

Section: Enzymes Of Fungal and Bacterial Originmentioning

confidence: 99%

The role of enzymes in the formation of meat and meat products

Khvostov,

Khryachkova,

Minaev

2024

Teor. prakt. pererab. mâsa (Print)

Self Cite

View full text Add to dashboard Cite

show abstract

Collagenases and their inhibitors: a review

Zhou

Jin

et al. 2023

Collagen & Leather

View full text Add to dashboard Cite

Hide and skin are complex tissue where the most abundant component is collagen. Matrix metalloproteinases and bacterial collagenases are two kinds of collagenases that can cleave the triple-helical domain of native fibrillar collagens. In this paper, the family members and domain composition of matrix metalloproteinases and bacterial collagenases are summarized. The catalytic mechanism of collagen hydrolysis by collagenases is described, and the methods adopted to date for investigating and regulating collagenases and their inhibitors are reviewed. Furthermore, the applications of collagenases and their inhibitors in biomedicine, food processing and the enzymatic unhairing process in the leather-making industry are presented. Graphical Abstract

show abstract

Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger

Song

Wang

et al. 2021

PLoS ONE

View full text Add to dashboard Cite

A predicted metalloproteinase gene, HypZn, was cloned from Aspergillus niger CGMCC 3.7193 and expressed in Pichia pastoris GS115, and the physicochemical characteristics of recombinant HypZn were investigated after separation and purification. The results showed that the specific activity of the purified HypZn reached 1859.2 U/mg, and the optimum temperature and pH value of HypZn were 35°C and 7.0, respectively. HypZn remained stable both at 40°C and at pH values between 5.0 and 8.0. The preferred substrate of HypZn was soybean protein isolates, and the Km and Vmax values were 21.5 μmol/mL and 4926.6 μmol/(mL∙min), respectively. HypZn was activated by Co2+ and Zn2+ and inhibited by Cu2+ and Fe2+. The degree of soybean protein isolate hydrolysis reached 14.7%, and the hydrolysates were of uniform molecular weight. HypZn could tolerate 5000 mM NaCl and completely lost its activity after 30 min at 50°C. The enzymological characterizations indicated that HypZn has great application potential in the food industry, especially in fermented food processing.

show abstract

Recombinant metalloprotease as a perspective enzyme for meat tenderization

Cited by 4 publications

References 19 publications

The role of enzymes in the formation of meat and meat products

The role of enzymes in the formation of meat and meat products

Collagenases and their inhibitors: a review

Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger

Contact Info

Product

Resources

About