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Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.).
J Sci Food Agric. 2010 Jan 30; 90(2):291-8.JS

Abstract

BACKGROUND

Thailand is the second largest surimi producer in the world and 50% of surimi is produced from threadfin bream. During surimi processing, sarcoplasmic proteins are removed through water washing and discarded in the waste stream. This study was aimed at investigating the proteinase inhibitory activity of sarcoplasmic proteins.

RESULTS

Sarcoplasmic proteins from threadfin bream (TBSP) exhibited inhibitory activity toward trypsin but did not inhibit papain and chymotrypsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing condition stained by trypsin inhibitory activity revealed three protein bands of molecular mass of 95, 41 and 37 kDa. Inhibitory activity of TBSP reached a maximum when subjected to 45 degrees C and completely disappeared at 60 degrees C. The breaking force and deformation of lizardfish surimi gel with added TBSP and pre-incubated at 37 degrees for 20 min increased with additional levels of TBSP (P < 0.05). Trichloroacetic acid-oligopeptide content of lizardfish surimi gel with added TBSP decreased with the addition of 4 g kg(-1) TBSP (P < 0.05). Retention of myosin heavy chain (MHC) increased when TBSP concentration was increased. TBSP effectively protected MHC from proteolysis at 37 degrees C to a similar extent as egg white powder, but efficacy of TBSP was not observed at 65 degrees C.

CONCLUSION

TBSP could be applied to reduce proteolytic degradation of lizardfish surimi or other surimi associated with trypsin-like proteinase, rendering an improvement in surimi gelation set at 37-40 degrees C.

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Authors+Show Affiliations

Piyadhammaviboon P
School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, Thailand.
Yongsawatdigul J
No affiliation info available

MeSH

AnimalsElectrophoresis, Polyacrylamide GelEnzymesFish ProductsFish ProteinsGelsHydrolysisMuscle ProteinsMyosin Heavy ChainsOligopeptidesPerciformesProtease InhibitorsSarcoplasmic ReticulumTemperatureTrichloroacetic Acid

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20355045

Citation

Piyadhammaviboon, Penprapha, and Jirawat Yongsawatdigul. "Proteinase Inhibitory Activity of Sarcoplasmic Proteins From Threadfin Bream (Nemipterus Spp.)." Journal of the Science of Food and Agriculture, vol. 90, no. 2, 2010, pp. 291-8.
Piyadhammaviboon P, Yongsawatdigul J. Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.). J Sci Food Agric. 2010;90(2):291-8.
Piyadhammaviboon, P., & Yongsawatdigul, J. (2010). Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.). Journal of the Science of Food and Agriculture, 90(2), 291-8. https://doi.org/10.1002/jsfa.3814
Piyadhammaviboon P, Yongsawatdigul J. Proteinase Inhibitory Activity of Sarcoplasmic Proteins From Threadfin Bream (Nemipterus Spp.). J Sci Food Agric. 2010 Jan 30;90(2):291-8. PubMed PMID: 20355045.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.). AU - Piyadhammaviboon,Penprapha, AU - Yongsawatdigul,Jirawat, PY - 2010/4/1/entrez PY - 2010/4/1/pubmed PY - 2010/9/23/medline SP - 291 EP - 8 JF - Journal of the science of food and agriculture JO - J Sci Food Agric VL - 90 IS - 2 N2 - BACKGROUND: Thailand is the second largest surimi producer in the world and 50% of surimi is produced from threadfin bream. During surimi processing, sarcoplasmic proteins are removed through water washing and discarded in the waste stream. This study was aimed at investigating the proteinase inhibitory activity of sarcoplasmic proteins. RESULTS: Sarcoplasmic proteins from threadfin bream (TBSP) exhibited inhibitory activity toward trypsin but did not inhibit papain and chymotrypsin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing condition stained by trypsin inhibitory activity revealed three protein bands of molecular mass of 95, 41 and 37 kDa. Inhibitory activity of TBSP reached a maximum when subjected to 45 degrees C and completely disappeared at 60 degrees C. The breaking force and deformation of lizardfish surimi gel with added TBSP and pre-incubated at 37 degrees for 20 min increased with additional levels of TBSP (P < 0.05). Trichloroacetic acid-oligopeptide content of lizardfish surimi gel with added TBSP decreased with the addition of 4 g kg(-1) TBSP (P < 0.05). Retention of myosin heavy chain (MHC) increased when TBSP concentration was increased. TBSP effectively protected MHC from proteolysis at 37 degrees C to a similar extent as egg white powder, but efficacy of TBSP was not observed at 65 degrees C. CONCLUSION: TBSP could be applied to reduce proteolytic degradation of lizardfish surimi or other surimi associated with trypsin-like proteinase, rendering an improvement in surimi gelation set at 37-40 degrees C. SN - 1097-0010 UR - https://www.unboundmedicine.com/medline/citation/20355045/Proteinase_inhibitory_activity_of_sarcoplasmic_proteins_from_threadfin_bream__Nemipterus_spp___ L2 - https://doi.org/10.1002/jsfa.3814 DB - PRIME DP - Unbound Medicine ER -