摘要:

ABSTRACTEvidence suggests that both the myofibrillar proteins and collagen play important roles in meat flavor and tenderness. The probable contributions of the purified proteins to flavor are reviewed in terms of their amino acid composition, especially the sulfur containing and certain other amino acids that have been implicated in meat flavor development. Myofibrils solubilized in sodium dodecylsulfate (SDS) undergoproteolysis on warming to room temperature overnight or on storing for several days at 0–4°C as demonstrated by extra protein bands. The extra proteins appear to be due to the presence of indigenous muscle proteases. The implications of some indigenous muscle proteases are reviewed in terms of their probable role in tenderization of postmortem me

ISSN:0145-8884    

DOI:10.1111/j.1745-4514.1983.tb00798.x

出版商:Blackwell Publishing Ltd    

年代:1983

数据来源: WILEY

摘要:

ABSTRACTThe central role of Ca2+in the regulation of muscular activity is well documented. At the level of the contractile proteins the dominant effect of Ca2+is attributable to the Ca2+‐bindingprotein, troponin C. This protein in the presence of Ca2+elicits conformational changes which allow cross‐bridge cycling and hence contraction. Another Ca2+‐binding protein, similar in its physical properties to troponin C, has also been discovered and this is calmodulin. The latter differs from troponin C in that it is involved in the regulation of a wide range of enzymatic reactions and it appears to be a ubiquitous regulatory protein. In skeletal muscle, as in all other eukaryotic cells, the number of calmodulin‐dependent systems is too large to be considered and only two enzymes have been selected. These are myosin light chain kinase and phosphory lose kinase. The activities of both are intimately related to the contractile mechanism and for this reason their actions could be important to meat

ISSN:0145-8884    

DOI:10.1111/j.1745-4514.1983.tb00799.x

出版商:Blackwell Publishing Ltd    

年代:1983

数据来源: WILEY

摘要:

ABSTRACTFrom a review of the literature, and from specific data presented in this paper, it was concluded that both postmortem temperature and pH have effects on meat tenderness and on disruption of specific myofibrillar proteins. Increased postmortem temperature porduces more tender muscles and increases the disruption of troponin‐T, myosin, Z‐lines, connectin and gap filaments. Elevated postmortem temperature also increases the activity of enzymes which cause the disruption of myofibrillar proteins. Higher ultimate postmortem pH (above 6.0) produces more tender muscle, but also produces dark‐cutting meat Except for one experiment, lower pH in the first few hours postmortem (in muscle with normal ultimate pH; i.e., 5.8 or below) improves meat tenderness. High pH increases the activity of CAF and low pH increases the activity of lsosomal cathepsins. Both high and low pH increase the degradation of troponin‐T, Z‐lines, gap filaments and connectin, but the degradation of these proteins (except for Z‐lines) is greater at a low pH. Low pH increases the degradation of myosin; conversely, high pH retards it

ISSN:0145-8884    

DOI:10.1111/j.1745-4514.1983.tb00800.x

出版商:Blackwell Publishing Ltd    

年代:1983

数据来源: WILEY

摘要:

ABSTRACTA 42,000 dalton protein has been identified in chicken breast muscle which differs from actin in that it is soluble at low ionic strength and insoluble in 1 MKI solutions. This protein is readily hydrolysed by Ca++‐activated neutral protease from chicken breast muscle, and is not present in Ca++‐activated neutral protease treated myofibrils. This protein may be involved in the integrity of the Z—disc in skeletal m

ISSN:0145-8884    

DOI:10.1111/j.1745-4514.1983.tb00801.x

出版商:Blackwell Publishing Ltd    

年代:1983

数据来源: WILEY

摘要:

Book reviewed in this article:Prescott&Dunn's Industrial Microbiology. 4th Edition, G. Reed, Ed., Avi Publishing Company

ISSN:0145-8884    

DOI:10.1111/j.1745-4514.1983.tb00802.x

出版商:Blackwell Publishing Ltd    

年代:1983

数据来源: WILEY