Comparative study on degradation, aggregation and rheological properties of actomyosin from cold, temperate and warm water fish species
Yükleniyor...
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Bu çalışmada, Alaska pollock (Theragra chalcogramma), Pacific whiting (Merluccius productus), bigeye snapper (Priacanthus spp.), lizardfish (Saurida spp.) ve threadfin bream (Nemipterus spp.) surimilerinden hazırlanan aktomyozinin proteolitik parçalanma ve ısıl topaklanma eğilimi ve reolojik özellikleri karşılaştırmalı olarak incelenmiştir. Arıtılmamış aktomyozin örneklerinde belirgin bir endojen proteolitik aktivite görülürken, Pacific whiting ve lizardfish en yüksek proteolitik aktiviteyi göstermişlerdir. SDS-PAGE analizi, Pacific whiting, bigeye snapper, lizardfish ve threadfin bream miyozin ağır zincir bantlarının yoğunluğunun inkübasyon süresi uzadıkça azaldığını, orta ve düşük molekül ağırlıklı proteinlerin oluştuğunu göstermiştir. Test edilen bütün balık türleri için 0,5°C dk–1 ısıtma hızı daha yüksek bulanıklık değerlerine neden olurken, bunu 1,0°C dk–1 ve daha sonra 2,0°C dk–1 ısıtma hızları izlemiştir. Bulanıklığın artmaya başladığı sıcaklık değeri balık türünden belirgin bir şekilde etkilenmiştir. Aktomyozinin sıcaklık tarama testlerinden elde edilen dinamik depolama modülü pik sıcaklıklarının diferansiyel taramalı kolorimetre geçiş sıcaklık değerlerine yakın olduğu görülmüştür. Bu, dinamik testlerden elde edilen piklerin protein denatürasyon sıcaklıkları ile ilgili olduğuna işaret etmektedir. Düşük ısıtma hızları, ısıl geçiş sıcaklığının daha düşük bir değere kaydırmıştır. Bu sonuçlar, protein jeli oluşum özellikleri ve proteolitik parçalanma açısından balık türlerinin ısıl hassasiyetinin daha iyi anlaşılmasını sağlayacaktır.
Proteolytic degradation and thermal aggregation patterns and dynamic rheological properties of actomyosin prepared from Alaska pollock (Theragra chalcogramma), Pacific whiting (Merluccius productus), bigeye snapper (Priacanthus spp.), lizardfish (Saurida spp.) and threadfin bream (Nemipterus spp.) surimi were comparatively studied. There was a significant endogenous protease activity observed in crude actomyosin samples where Pacific whiting and lizardfish exhibited the highest proteolytic activity. SDS-PAGE analysis showed that intensity of myosin heavy chain bands of Pacific whiting, bigeye snapper, lizardfish and threadfin bream decreased with extended incubation time, resulting in medium and low molecular weight proteins. For all tested fish species, a 0.5°C min–1 heating rate resulted in higher turbidity values followed by 1.0°C min–1 and then 2.0°C min–1. Temperature onset point for turbidity increase was significantly affected by species. Storage modulus peak temperatures, obtained from temperature sweep tests of actomyosins, were similar to thermal transition values obtained from differential scanning calorimetry, indicating that peaks obtained from the dynamic tests were related to protein denaturation temperatures. Slower heating rate shifted the thermal transition temperature to a lower value. These observations should give better understanding of the thermal sensitivity of fish species with regards to gelation properties and proteolytic degradation.
Proteolytic degradation and thermal aggregation patterns and dynamic rheological properties of actomyosin prepared from Alaska pollock (Theragra chalcogramma), Pacific whiting (Merluccius productus), bigeye snapper (Priacanthus spp.), lizardfish (Saurida spp.) and threadfin bream (Nemipterus spp.) surimi were comparatively studied. There was a significant endogenous protease activity observed in crude actomyosin samples where Pacific whiting and lizardfish exhibited the highest proteolytic activity. SDS-PAGE analysis showed that intensity of myosin heavy chain bands of Pacific whiting, bigeye snapper, lizardfish and threadfin bream decreased with extended incubation time, resulting in medium and low molecular weight proteins. For all tested fish species, a 0.5°C min–1 heating rate resulted in higher turbidity values followed by 1.0°C min–1 and then 2.0°C min–1. Temperature onset point for turbidity increase was significantly affected by species. Storage modulus peak temperatures, obtained from temperature sweep tests of actomyosins, were similar to thermal transition values obtained from differential scanning calorimetry, indicating that peaks obtained from the dynamic tests were related to protein denaturation temperatures. Slower heating rate shifted the thermal transition temperature to a lower value. These observations should give better understanding of the thermal sensitivity of fish species with regards to gelation properties and proteolytic degradation.
Açıklama
Anahtar Kelimeler
Zooloji, Balıkçılık
Kaynak
Turkish Journal of Fisheries and Aquatic Sciences
WoS Q Değeri
Q4
Scopus Q Değeri
Q2
Cilt
14
Sayı
1
