Biochemical characterization of a novel lipase from Malbranchea cinnamomea suitable for production of lipolyzed milkfat flavor and biodegradation of phthalate esters

Xiaojie Duan; Man Xiang; Ling Wang; Qiaojuan Yan; Shaoqing Yang; Zhengqiang Jiang

doi:10.1016/j.foodchem.2019.05.199

Biochemical characterization of a novel lipase from Malbranchea cinnamomea suitable for production of lipolyzed milkfat flavor and biodegradation of phthalate esters

Food Chem. 2019 Nov 1:297:124925. doi: 10.1016/j.foodchem.2019.05.199. Epub 2019 May 31.

Authors

Xiaojie Duan¹, Man Xiang², Ling Wang³, Qiaojuan Yan⁴, Shaoqing Yang⁵, Zhengqiang Jiang⁶

Affiliations

¹ Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; College of Food Science and Technology, Henan University of Technology, Zhengzhou 450001, China. Electronic address: henanduanxiaojie@163.com.
² Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: manx@cau.edu.cn.
³ Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: wangle@cau.edu.cn.
⁴ Bioresource Utilization Laboratory, College of Engineering, China Agricultural University, Beijing 100083, China. Electronic address: yanqj@cau.edu.cn.
⁵ Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: ysq@cau.edu.cn.
⁶ Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China. Electronic address: zhqjiang@cau.edu.cn.

PMID: 31253266
DOI: 10.1016/j.foodchem.2019.05.199

Abstract

A novel lipase gene (McLipB) was cloned from a thermophilic fungus Malbranchea cinnamomea and expressed in Pichia pastoris. The deduced amino acid sequence of the lipase (McLipB) shared the highest identity of 46% with the Candida rugosa lipase LIP4. The extracellular lipase activity of 4304 U/mL with protein concentration of 7.7 mg/mL was achieved in a 5-L fermentor. The optimal pH and temperature of McLipB were 7.5 and 40 °C, respectively. The lipase showed high specificity towards triglycerides with short and medium chain fatty acids, and had non-position specificity. McLipB hydrolyzed butter to produce mainly butyric acid, hexanoic acid and a small amount of octanoic acid and decanoic acid. Furthermore, it degraded more than 90% dipropyl phthalate, dibutyl phthalate and dihexyl phthalate to their corresponding monoalkyl phthalates. The properties of McLipB indicate that it has great application potential for production of lipolyzed milkfat flavor and biodegradation of phthalate esters.

Keywords: Biochemical characterization; Lipase; Lipolyzed milkfat flavor; Malbranchea cinnamomea; Phthalate esters.

MeSH terms

Amino Acid Sequence
Ascomycota / enzymology*
Batch Cell Culture Techniques
Candida / enzymology
Hydrogen-Ion Concentration
Hydrolysis
Lipase / chemistry
Lipase / genetics
Lipase / metabolism*
Phthalic Acids / chemistry
Phthalic Acids / metabolism
Pichia / metabolism
Recombinant Proteins / biosynthesis
Recombinant Proteins / chemistry
Recombinant Proteins / isolation & purification
Sequence Alignment
Substrate Specificity
Temperature
Triglycerides / metabolism

Substances

Phthalic Acids
Recombinant Proteins
Triglycerides
Lipase