Sanden Karen Wahlstrøm, Böcker Ulrike, Ofstad Ragni, Pedersen Mona Elisabeth, Høst Vibeke, Afseth Nils Kristian, Rønning Sissel Beate, Pleshko Nancy
Nofima AS, Muninbakken 9-13, Breivika, 9019 Tromsø, Norway.
Department of Bioengineering, Temple University, Philadelphia, PA 19122, USA.
Foods. 2021 Mar 6;10(3):548. doi: 10.3390/foods10030548.
Recently, two chicken breast fillet abnormalities, termed Wooden Breast (WB) and Spaghetti Meat (SM), have become a challenge for the chicken meat industry. The two abnormalities share some overlapping morphological features, including myofiber necrosis, intramuscular fat deposition, and collagen fibrosis, but display very different textural properties. WB has a hard, rigid surface, while the SM has a soft and stringy surface. Connective tissue is affected in both WB and SM, and accordingly, this study's objective was to investigate the major component of connective tissue, collagen. The collagen structure was compared with normal (NO) fillets using histological methods and Fourier transform infrared (FTIR) microspectroscopy and imaging. The histology analysis demonstrated an increase in the amount of connective tissue in the chicken abnormalities, particularly in the perimysium. The WB displayed a mixture of thin and thick collagen fibers, whereas the collagen fibers in SM were thinner, fewer, and shorter. For both, the collagen fibers were oriented in multiple directions. The FTIR data showed that WB contained more β-sheets than the NO and the SM fillets, whereas SM fillets expressed the lowest mature collagen fibers. This insight into the molecular changes can help to explain the underlying causes of the abnormalities.
最近,两种鸡胸肉异常情况,即木鸡胸(WB)和意大利面状肉(SM),已成为鸡肉行业面临的一项挑战。这两种异常情况具有一些重叠的形态学特征,包括肌纤维坏死、肌内脂肪沉积和胶原纤维化,但呈现出截然不同的质地特性。WB的表面坚硬、僵硬,而SM的表面柔软且呈丝状。WB和SM中的结缔组织均受到影响,因此,本研究的目的是调查结缔组织的主要成分——胶原蛋白。使用组织学方法以及傅里叶变换红外(FTIR)显微光谱和成像技术,将胶原蛋白结构与正常(NO)鸡胸肉进行了比较。组织学分析表明,鸡肉异常情况中结缔组织的数量有所增加,尤其是在肌束膜中。WB呈现出细胶原纤维和粗胶原纤维的混合,而SM中的胶原纤维更细、数量更少且更短。对于这两种情况,胶原纤维均呈多个方向排列。FTIR数据显示,WB比NO和SM鸡胸肉含有更多β折叠,而SM鸡胸肉中成熟胶原纤维的含量最低。对这些分子变化的深入了解有助于解释这些异常情况的潜在原因。