“Rigid” structure is a key determinant for the low digestibility of myoglobin

Myoglobin, a critical protein responsible for meat color, has been shown insusceptible to digestion. The underlying mechanism is not clear. The present study aimed to evaluate whether the structural properties of myoglobin are associated with its insusceptibility to digestion using spectroscopic and...

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Main Authors:	Qian Li, Di Zhao, Hui Liu, Miao Zhang, Shuai Jiang, Xinglian Xu, Guanghong Zhou, Chunbao Li
Format:	Article
Language:	English
Published:	Elsevier 2020-09-01
Series:	Food Chemistry: X
Subjects:	Myoglobin Digestibility Molecular dynamics Molecular docking Liquid chromatography-tandem mass spectrometry
Online Access:	http://www.sciencedirect.com/science/article/pii/S2590157520300183

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spelling	doaj-677eb1d723e141d2b5c15c0c0485165e2020-11-25T02:55:05ZengElsevierFood Chemistry: X2590-15752020-09-017100094“Rigid” structure is a key determinant for the low digestibility of myoglobinQian Li0Di Zhao1Hui Liu2Miao Zhang3Shuai Jiang4Xinglian Xu5Guanghong Zhou6Chunbao Li7Key Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaKey Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaCorresponding author at: College of Food Science and Technology, Nanjing Agricultural University, Weigang 1#, Nanjing 210095, China.; Key Laboratory of Meat Processing and Quality Control, MOE, Key Laboratory of Meat Processing, MARA, Jiangsu Collaborative Innovation Center of Meat Production, Processing and Quality Control, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, ChinaMyoglobin, a critical protein responsible for meat color, has been shown insusceptible to digestion. The underlying mechanism is not clear. The present study aimed to evaluate whether the structural properties of myoglobin are associated with its insusceptibility to digestion using spectroscopic and computational techniques. Myoglobin was degraded by only 7.03% by pepsin and 33.00% by pancreatin. The structure of myoglobin still maintained α-helix after the two-step digestion, with the exposure of some aromatic residues. In addition, molecular dynamics modeling suggested that hydrophobic amino acid residues (Phe 111, Leu 10, Ala 115, Pro 116) in pepsin and polar amino acid residues (Tyr 146, Thr 95) in myoglobin were found in the proximity of binding sites, which could result in the low digestibility of myoglobin. Our findings provide a new insight into the underlying mechanisms on the difficulty in digestion of myoglobin.http://www.sciencedirect.com/science/article/pii/S2590157520300183MyoglobinDigestibilityMolecular dynamicsMolecular dockingLiquid chromatography-tandem mass spectrometry
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Qian Li Di Zhao Hui Liu Miao Zhang Shuai Jiang Xinglian Xu Guanghong Zhou Chunbao Li
spellingShingle	Qian Li Di Zhao Hui Liu Miao Zhang Shuai Jiang Xinglian Xu Guanghong Zhou Chunbao Li “Rigid” structure is a key determinant for the low digestibility of myoglobin Food Chemistry: X Myoglobin Digestibility Molecular dynamics Molecular docking Liquid chromatography-tandem mass spectrometry
author_facet	Qian Li Di Zhao Hui Liu Miao Zhang Shuai Jiang Xinglian Xu Guanghong Zhou Chunbao Li
author_sort	Qian Li
title	“Rigid” structure is a key determinant for the low digestibility of myoglobin
title_short	“Rigid” structure is a key determinant for the low digestibility of myoglobin
title_full	“Rigid” structure is a key determinant for the low digestibility of myoglobin
title_fullStr	“Rigid” structure is a key determinant for the low digestibility of myoglobin
title_full_unstemmed	“Rigid” structure is a key determinant for the low digestibility of myoglobin
title_sort	“rigid” structure is a key determinant for the low digestibility of myoglobin
publisher	Elsevier
series	Food Chemistry: X
issn	2590-1575
publishDate	2020-09-01
description	Myoglobin, a critical protein responsible for meat color, has been shown insusceptible to digestion. The underlying mechanism is not clear. The present study aimed to evaluate whether the structural properties of myoglobin are associated with its insusceptibility to digestion using spectroscopic and computational techniques. Myoglobin was degraded by only 7.03% by pepsin and 33.00% by pancreatin. The structure of myoglobin still maintained α-helix after the two-step digestion, with the exposure of some aromatic residues. In addition, molecular dynamics modeling suggested that hydrophobic amino acid residues (Phe 111, Leu 10, Ala 115, Pro 116) in pepsin and polar amino acid residues (Tyr 146, Thr 95) in myoglobin were found in the proximity of binding sites, which could result in the low digestibility of myoglobin. Our findings provide a new insight into the underlying mechanisms on the difficulty in digestion of myoglobin.
topic	Myoglobin Digestibility Molecular dynamics Molecular docking Liquid chromatography-tandem mass spectrometry
url	http://www.sciencedirect.com/science/article/pii/S2590157520300183
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“Rigid” structure is a key determinant for the low digestibility of myoglobin

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