iTRAQ-based quantitative proteomic analysis of the effect of heat shock on freeze-drying of Lactobacillus acidophilus ATCC4356

被引：3

作者：

Liu, Mingxue ^{[1
,2
]}

Zeng, Xiaoqun ^{[1
,2
]}

He, Yating ^{[1
,2
]}

Xia, Chaoran ^{[1
,2
]}

Cheng, Lu ^{[1
,2
]}

Wu, Zhen ^{[1
,2
]}

Lan, Hangzhen ^{[1
,2
]}

Pan, Daodong ^{[1
,2
]}

机构：

[1] State Key Lab Managing Biot & Chem Threats Qual &, Ningbo 315211, Peoples R China

[2] Ningbo Univ, Key Lab Anim Prot Food Proc Technol Zhejiang Prov, Coll Food & Pharmaceut Sci, Ningbo 315800, Peoples R China

来源：

INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY | 2021年 / 56卷 / 11期

基金：

中国国家自然科学基金;

关键词：

freeze-drying; glycolysis; heat shock; iTRAQ; Lactobacillus acidophilus; HIBERNATING 100S RIBOSOME; LACTOCOCCUS-LACTIS; CRYOPROTECTIVE MEDIUM; STRESS RESISTANCE; MEMBRANE; STABILITY; VIABILITY; SURVIVAL; GROWTH; OPTIMIZATION;

D O I：

10.1111/ijfs.15101

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

In order to investigate the mechanism by which heat shock improves the survival rate of lactic acid bacteria (LAB) following lyophilisation, we performed proteomic analysis based on isobaric tags for relative and absolute quantitation (iTRAQ) on Lactobacillus acidophilus (LA) ATCC4356. Among the 75 differentially expressed proteins (DEPs), 16 and 59 were up- and downregulated, respectively, mainly related to amino acid metabolism, glycolysis, ABC transportation, transcription and translation. MrnC, tuf, recG, ychF, purB, dtpT, LBA1220, LBA0434 and LBA0921 were identified as key genes mediating tolerance to freeze-drying. Energy supply was enhanced by regulating amino acid metabolism and glycolysis, while energy consumption was decreased by downregulating most translation-related proteins. DNA and the cellular internal environment were stabilised, and ABC transporters assisted adaptation to freeze-drying. The results provide new insight for understanding tolerance to freeze-drying in LAB following heat shock treatment.

引用

页码：5569 / 5580

页数：12

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