Effect of lactic or acetic acid on degradation of myofibrillar proteins in post-mortem goose (Anser anser) breast muscle

Hwang, Ing-Haur; Lin, Chin‐Wen; Chou, Rong‐Ghi R.

doi:10.1002/(sici)1097-0010(20000115)80:2<231::aid-jsfa521>3.0.co;2-l

Cited by 11 publications

(11 citation statements)

References 33 publications

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“…Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) has found wide application and is used to monitor the proteolytic degradation of myofibrils during post-mortem storage of the meat of many different animal species. It is aIso commonly used to study chemical interactions in gelation of muscle proteins (Hwang et al, 2000;Toyohara et al, 1990;Koohrnaraie et al, 1984;Weber and Osborn, 1969).…”

Section: Fats and Oilssupporting

confidence: 91%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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: The changes in protein structure associated with the preparation and frozen storage of surimi were investigated. Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled water. The product was either slowly frozen or underwent rapid freezing using liquid air; in either case it was then subjected to frozen storage at ‐20 °C for 24 mo. Fourier transform infrared/attenuated total reflectance (FTIR/ATR) spectroscopy showed that during preparation of surimi, the a‐helix content increased with increased number of washing cycles. Differential scanning calorimetry (DSC) revealed a shift in the thermal transition of actin to a higher temperature during surimi preparation. Electrophoresis, FTIR/ATR spectroscopy, and DSC results revealed a loss of myofibrillar proteins from surimi after 3 washing cycles, suggesting that 3 washing cycles were adequate to prepare surimi. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) showed relatively minor changes in protein subunit structure with some loss of the myosin light chains (MLC); myosin heavy chain (MHC), actin, and tropomyosin were found to be relatively stable. Native‐PAGE showed no major changes in surimi after 24 mo storage at ‐20 °C. FTIR/ ATR spectroscopy indicated a significant decrease in a‐helix relative to p‐sheet structure in surimi after 2 y of storage at ‐20 °C. The loss of α‐helical content was more significant in slowly frozen surimi compared with rapid‐frozen surimi samples. DSC results revealed a shift in the thermal transition of actin to lower temperatures during frozen storage of surimi.

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Section: Fats and Oilssupporting

confidence: 91%

Protein Structural Changes During Preparation and Storage of Surimi

Moosavi‐Nasab

Alli

Ismail

et al. 2005

Journal of Food Science

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“…Similar results were reported by other authors who found a decrease in the myosin band in fermented (Morzel et al. 2000) or acid‐treated meat (Hwang et al. 2000) stored under refrigeration.…”

Section: Resultssupporting

confidence: 91%

“…These endogenous enzymes generally play a major role in myofibrillar protein degradation at low pH (Schwartz and Bird 1977; Zeece et al 1986Zeece et al , 1992. Similar results were reported by other authors who found a decrease in the myosin band in fermented (Morzel et al 2000) or acid-treated meat (Hwang et al 2000) stored under refrigeration. The lysosome system contains 15-20 proteases and is one of several mechanisms of muscle protein intracellular degradation; the optimum pH for proteolytic activity is 3-4, although several enzymes of this group have a broader pH activity range (Zeece et al 1992).…”

Section: Effect Of Lactic Acid and Lab On Protein Degradationsupporting

confidence: 92%

Effect of Lactic Acid and Lactic Acid Bacteria Treatment on Myofibrillar Protein Degradation and Dynamic Rheology of Beef

Signorini

Salazar

Ponce‐Alquicira

et al. 2007

Journal of Texture Studies

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Lactic acid has been used as an efficient decontaminant in meats aimed for direct consumption or product fabrication. However, reports on the functionality of proteins extracted from lactic acid‐treated meat are scattered. The objective of this work was to study the degradation and gelling ability of myofibrillar protein extracts obtained from beef treated with lactic acid of chemical and microbial origins, stored at 4 and 20C. The gelling ability was considerably reduced by lactic acid treatment as a result of protein denaturation in acid conditions at both storage temperatures. Scanning electron microscopy showed loose structures resulting in low penetration resistance and storage modulus. Treatments with lactic acid or lactic acid bacteria (LAB) had similar effect on tanδ, affecting gel rigidity but not elasticity. Penetration in gels obtained from LAB‐treated meat was highly correlated with myosin degradation. Lactobacillus carnis‐treated meat produced compact gels with high penetration resistance and storage modulus, although the structure became looser with storage time. LAB treatment, although not as efficient as lactic acid as a meat preservative, is a milder process causing less severe changes in meat structure rheology. PRACTICAL APPLICATIONS The potential of lactic fermentation by selected strains is somewhat limited as compared to lactic acid preservation of meat substrates, regarding pH reduction and its consequence on pathogens and spoilage microorganism population reduction. However, lactic acid bacteria (LAB) treatments are milder; therefore, changes in protein structure and rheology are less severe. Lactic acid in its chemical form promotes protein changes, whereas LAB does not. As myofibrillar protein configuration is responsible for most meat functional properties, such as gel and emulsion formation, it is important that protein structure remains unchanged as much as possible. Using nonproteolytic strains, protein degradation can only be altered by endogenous or bacteria‐produced enzymes, which can be inhibited by several means. Meat preservation by lactic fermentation with selected strains can be an alternative when keeping meat protein functional properties unaltered.

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“…1.1. This agrees with the literature, which explains this swelling by acid penetration into intracellular and intercellular spaces (Gault, 1991;Hwang et al, 2000). Rao et al (1989b) demonstrated that below pH 4-5, the further pH falls, the more muscle swells.…”

Section: Study Of Mass Transfermentioning

confidence: 99%

“…2 also demonstrates that for NaCl molalities greater than 0.3, and probably up to 1 mol kg À1 , for durations of more than the 5 h of the study domain, we could have achieved more limited mass losses, or even obtained swelling for NaCl molalities from 0.5 to 0.7. This agrees with the literature, where immersion treatments are generally applied over at least 24 h before mass equilibrium is reached (Gault, 1985;Hwang et al, 2000;Karlsson et al, 1996). Going on Fig.…”

Section: Study Of Mass Transfermentioning

confidence: 99%