title: Molecular characterization of a thermophilic endo-polygalacturonase from Thielavia arenaria XZ7 with high catalytic efficiency and application potential in the food and feed industries.
abstract: Thermophilic endo-polygalacturonases with high catalytic efficiency are of great interest in the food and feed industries. This study identified an endo-polygalacturonase gene (pg7fn) of glycoside hydrolase family 28 in the thermophilic fungus Thielavia arenaria XZ7. Recombinant PG7fn produced in Pichia pastoris is distinguished from other enzyme counterparts by its high functional temperature (60 °C) and specific activity (34382 ± 351 U/mg toward polygalacturonic acid). The enzyme exhibited good pH stability (pH 3.0-8.0) and resistance to pepsin and trypsin digestion and had a significant effect on disaggregation of soybean meal. Addition of 1 U/g PG7fn increased the pectin bioavailability by 19.33%. The excellent properties described above make PG7fn valuable for applications in the food and feed industries. Furthermore, a comparative study showed that N-glycosylation improved the thermostability and catalytic efficiency of PG7fn.
authors.affiliation: Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences , Beijing 100081, People's Republic of China.
authors.forename: Tao
authors.initials: T
authors.lastname: Tu
authors.forename: Kun
authors.initials: K
authors.lastname: Meng
authors.forename: Huoqing
authors.initials: H
authors.lastname: Huang
authors.forename: Huiying
authors.initials: H
authors.lastname: Luo
authors.forename: Yingguo
authors.initials: Y
authors.lastname: Bai
authors.forename: Rui
authors.initials: R
authors.lastname: Ma
authors.forename: Xiaoyun
authors.initials: X
authors.lastname: Su
authors.forename: Pengjun
authors.initials: P
authors.lastname: Shi
authors.forename: Peilong
authors.initials: P
authors.lastname: Yang
authors.forename: Yaru
authors.initials: Y
authors.lastname: Wang
authors.forename: Bin
authors.initials: B
authors.lastname: Yao
mesh_terms: D000595:Amino Acid Sequence; D000821:Animal Feed / Q000032:analysis; D055162:Biocatalysis; D003001:Cloning, Molecular; D004795:Enzyme Stability; D019649:Food Industry; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010368:Pectins / Q000378:metabolism; D010843:Pichia / Q000235:genetics; D011096:Polygalacturonase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D020037:Sordariales / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics
chemical_list: D005656:Fungal Proteins; D010368:Pectins; D011096:Polygalacturonase
keywords: N-glycosylation; Thielavia arenaria XZ7; catalytic efficiency; endo-polygalacturonase; thermophilic