Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: Research note

Hongguo Jin; Youling Xiong; Zengqi Peng; Yan He; Rongrong Wang; Guanghong Zhou

doi:10.1016/j.meatsci.2010.10.014

Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: Research note

Hongguo Jin
, Youling Xiong
, Zengqi Peng
, Yan He
, Rongrong Wang
, Guanghong Zhou

Animal and Food Sciences

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

6 Scopus citations

Abstract

In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35°C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg²⁺ and Ca²⁺ levels, whose optimal concentrations were determined to be 3 and 6mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na⁺ and KIO₃, and was slightly activated by EDTA-2Na⁺. These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.

Original language	English
Pages (from-to)	372-376
Number of pages	5
Journal	Meat Science
Volume	89
Issue number	4
DOIs	https://doi.org/10.1016/j.meatsci.2010.10.014
State	Published - Dec 2011

Bibliographical note

Funding Information:
This work was supported by the Natural Science Foundation Program in Jiangsu Province of China ( BK2006146 ).

Funding

This work was supported by the Natural Science Foundation Program in Jiangsu Province of China ( BK2006146 ).

Funders	Funder number
Natural Science Foundation Program in Jiangsu Province of China	BK2006146

Keywords

Hydrolysis
Myosin
Tripolyphosphatase
Tripolyphosphate

ASJC Scopus subject areas

Food Science

Access to Document

10.1016/j.meatsci.2010.10.014

Cite this

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title = "Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: Research note",

abstract = "In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35°C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg2+ and Ca2+ levels, whose optimal concentrations were determined to be 3 and 6mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na+ and KIO3, and was slightly activated by EDTA-2Na+. These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.",

keywords = "Hydrolysis, Myosin, Tripolyphosphatase, Tripolyphosphate",

author = "Hongguo Jin and Youling Xiong and Zengqi Peng and Yan He and Rongrong Wang and Guanghong Zhou",

note = "Funding Information: This work was supported by the Natural Science Foundation Program in Jiangsu Province of China ( BK2006146 ).",

year = "2011",

month = dec,

doi = "10.1016/j.meatsci.2010.10.014",

language = "English",

volume = "89",

pages = "372--376",

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T1 - Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle

T2 - Research note

AU - Jin, Hongguo

AU - Xiong, Youling

AU - Peng, Zengqi

AU - He, Yan

AU - Wang, Rongrong

AU - Zhou, Guanghong

N1 - Funding Information: This work was supported by the Natural Science Foundation Program in Jiangsu Province of China ( BK2006146 ).

PY - 2011/12

Y1 - 2011/12

N2 - In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35°C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg2+ and Ca2+ levels, whose optimal concentrations were determined to be 3 and 6mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na+ and KIO3, and was slightly activated by EDTA-2Na+. These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.

AB - In this study, we investigated the tripolyphosphatase (TPPase) activity responsible for the hydrolysis of tripolyphosphates (TPP) in rabbit Psoas major muscle tissue. After a series of extraction and purification steps, myosin was identified to be a TPPase. Optimum pH and temperature for myosin-TPPase activity were 6.0 and 35°C, respectively. We also found that myosin-TPPase activity was significantly influenced by Mg2+ and Ca2+ levels, whose optimal concentrations were determined to be 3 and 6mM, respectively. Furthermore, myosin-TPPase was strongly inhibited by EDTA-4Na+ and KIO3, and was slightly activated by EDTA-2Na+. These results suggest that it may be useful to regulate tripolyphosphate hydrolysis to enhance its function in meat processing.

KW - Hydrolysis

KW - Myosin

KW - Tripolyphosphatase

KW - Tripolyphosphate

UR - https://www.scopus.com/pages/publications/80051842378

UR - https://www.scopus.com/pages/publications/80051842378#tab=citedBy

U2 - 10.1016/j.meatsci.2010.10.014

DO - 10.1016/j.meatsci.2010.10.014

M3 - Article

C2 - 21689892

AN - SCOPUS:80051842378

SN - 0309-1740

VL - 89

SP - 372

EP - 376

JO - Meat Science

JF - Meat Science

IS - 4

ER -

Purification and characterization of myosin-tripolyphosphatase from rabbit Psoas major muscle: Research note

Abstract

Bibliographical note

Funding

Keywords

ASJC Scopus subject areas

Access to Document

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