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Development of a rapid method to detect bovine myosin isoforms in comminuted meat products and determine their relationship to bind
Abstract
Myosin isolates from bovine sternomandibularis (sm), masseter (ma) and rectus abdominis (ra) (mixed fiber type, homogenously slow fiber type and predominantly fast fiber type, respectively) were prepared and used as antigens to develop polyclonal and monoclonal antibodies. Two Enzyme Linked Immunosorbent Assays (ELISA's) were developed to quantitate the total amount of myosin and the fast (Type II) isoforms of myosin in muscle extracts. Results of the ELISA tests and functionality assays for texture and water holding capacity performed on frankfurters made from each muscle type were statistically analyzed to determine if differences could be detected in muscle types and if there was a relationship between the amount of total and/or fast myosin and the various measures of bind. Analysis of variance (ANOVA) indicated statistically significant ($\alpha$ =.05) differences between the homogenously slow (ma) muscle and the other two muscles containing both fast and slow fiber types including the amount of protein extracted, total myosin extracted and chewiness of the frankfurters. The predominantly white muscle (ra) was also shown to be significantly different from the ma and sm according to the emulsion stability test having the least amount of liquid after cooking. No significant relationships were indicated by Analysis of Covariance (ANCOVA) between the myosin or composition variables (TMP, TMW, TPE, MHCE, MHCT, TMPE, TMPT, TMWE, TMWT, FAT1, PRO1, MOIST1) and measurements of bind (TVOL, FAT, WATER, CPR, HARD, SPRING, COHES, CHEWY).
Subject Area
Food science
Recommended Citation
Krueger, Rebecca Ruth, "Development of a rapid method to detect bovine myosin isoforms in comminuted meat products and determine their relationship to bind" (1993). ETD collection for University of Nebraska-Lincoln. AAI9415975.
https://digitalcommons.unl.edu/dissertations/AAI9415975