2006
DOI: 10.1016/j.foodres.2006.07.008
|View full text |Cite
|
Sign up to set email alerts
|

Some physico-chemical, functional and rheological properties of actomyosin from green mussel (Perna viridis)

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
17
0

Year Published

2012
2012
2023
2023

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 16 publications
(19 citation statements)
references
References 35 publications
2
17
0
Order By: Relevance
“…The values of n 0 of YAM and GAM gels were smaller than that of actomyosin solutions before heating, indicating that the network of actomyosin solution is far from its developed stable gel state. A similar effect has been reported by Binsi et al [34] for actomyosin from 5 Protein concentration dependence of gelation temperature of actomyosin from yellowcheek carp and grass carp green mussels. The values of n 0 of actomyosin solution and gel from green mussels were 0.2803 and 0.0138, respectively.…”
Section: Dependence Of Gelation Temperature On Actomyosin Concentrationsupporting
confidence: 86%
“…The values of n 0 of YAM and GAM gels were smaller than that of actomyosin solutions before heating, indicating that the network of actomyosin solution is far from its developed stable gel state. A similar effect has been reported by Binsi et al [34] for actomyosin from 5 Protein concentration dependence of gelation temperature of actomyosin from yellowcheek carp and grass carp green mussels. The values of n 0 of actomyosin solution and gel from green mussels were 0.2803 and 0.0138, respectively.…”
Section: Dependence Of Gelation Temperature On Actomyosin Concentrationsupporting
confidence: 86%
“…Another reason for the oxidative stability during pH shift processing could be the presence of carotenoids in the mussel meat. In fact, studies have shown that protein isolates and hydrolysates from crustaceans exhibit antioxidant properties owing to the presence of peptides and carotenoids 30, 43…”
Section: Discussionmentioning
confidence: 99%
“…Taskaya et al 25 reported no gelling ability of proteins recovered by the pH shift method from whole carp unless gel enhancers were added. In order to make comparisons with gels from other marine bivalve molluscs, one must go to studies on isolated green mussel ( Perna viridis ) actomyosin43 and paste from fresh scallop striated adductor muscle 51. Gels from both these materials were reported to have relatively weak gel‐forming ability as indicated by frequency sweep (i.e.…”
Section: Discussionmentioning
confidence: 99%
“…; Binsi et al . ). The residue left after extraction of sarcoplasmic and myofibrillar proteins is known as stromal protein (1.4% of total protein nitrogen) (Wilhelmsson et al .…”
Section: Resultsmentioning
confidence: 97%