A novel thermophile β-galactosidase from Thermothielavioides terrestris producing galactooligosaccharides from acid whey

被引:32
作者
Zerva, Anastasia [1 ]
Limnaios, Athanasios [2 ]
Kritikou, Anastasia S. [3 ]
Thomaidis, Nikolaos S. [3 ]
Taoukis, Petros [2 ]
Topakas, Evangelos [1 ]
机构
[1] Natl Tech Univ Athens, Sch Chem Engn, Biotechnol Lab, 5 Iroon Polytech Str,Zografou Campus, Athens 15780, Greece
[2] Natl Tech Univ Athens, Sch Chem Engn, Lab Food Chem & Technol, 5 Iroon Polytechniou Str,Zorgafou Campus, Athens 15780, Greece
[3] Natl & Kapodistrian Univ Athens, Dept Chem, Analyt Chem Lab, Athens 15771, Greece
关键词
Acid whey; -galactosidase; Galactooligosaccharides; Thermothielavioides terrestris; Thermophilic enzymes; MYCELIOPHTHORA-THERMOPHILA; KLUYVEROMYCES-LACTIS; LACTOSE HYDROLYSIS; PROTEINS; IDENTIFICATION; FAMILY;
D O I
10.1016/j.nbt.2021.03.002
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
?-Galactosidases are key enzymes in the food industry. Apart from the hydrolysis of the saccharide bond of lactose, they also catalyze transgalactosylation reactions, producing galactooligosaccharides (GOS) with prebiotic activity. Here we report the heterologous production in Pichia pastoris of a novel ?-galactosidase from the fungus Thermothielavioides terrestris. The enzyme (TtbGal1) was purified and characterized, showing optimal activity at 60 ?C and pH 4. TtbGal1 is thermostable, retaining almost full activity for 24 h at 50 ?C. It was applied to the production of GOS from defined lactose solutions and acid whey, a liquid waste from the Greek yoghurt industry, reaching yields of 19.4 % and 14.8 %, respectively. HILIC?ESI-QTOF-MS analysis revealed the production of GOS with up to 4 saccharide monomers. The results demonstrate efficient GOS production catalyzed by TtbGal1, valorizing acid whey, a waste with a heavy polluting load from the dairy industry.
引用
收藏
页码:45 / 53
页数:9
相关论文
共 51 条
  • [21] Expression and characterization of Kluyveromyces lactis β-galactosidase in Escherichia coli
    Kim, CS
    Ji, ES
    Oh, DK
    [J]. BIOTECHNOLOGY LETTERS, 2003, 25 (20) : 1769 - 1774
  • [22] Kumar S, 2016, MOL BIOL EVOL, V33, P1870, DOI [10.1093/molbev/msw054, 10.1093/molbev/msv279]
  • [23] SACCHAROMYCES-CEREVISIAE CELLS SECRETING AN ASPERGILLUS-NIGER BETA-GALACTOSIDASE GROW ON WHEY PERMEATE
    KUMAR, V
    RAMAKRISHNAN, S
    TEERI, TT
    KNOWLES, JKC
    HARTLEY, BS
    [J]. BIO-TECHNOLOGY, 1992, 10 (01): : 82 - 85
  • [24] CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4
    LAEMMLI, UK
    [J]. NATURE, 1970, 227 (5259) : 680 - +
  • [25] Characterisation of a thermostable family 42 β-galactosidase from Thermotoga maritima
    Li, Lite
    Zhang, Min
    Jiang, Zhengqiang
    Tang, Luo
    Cong, Qianqian
    [J]. FOOD CHEMISTRY, 2009, 112 (04) : 844 - 850
  • [26] The carbohydrate-active enzymes database (CAZy) in 2013
    Lombard, Vincent
    Ramulu, Hemalatha Golaconda
    Drula, Elodie
    Coutinho, Pedro M.
    Henrissat, Bernard
    [J]. NUCLEIC ACIDS RESEARCH, 2014, 42 (D1) : D490 - D495
  • [27] Crystal structures of Trichoderma reesei β-galactosidase reveal conformational changes in the active site
    Maksimainen, Mirko
    Hakulinen, Nina
    Kallio, Johanna M.
    Timoharju, Tommi
    Turunen, Ossi
    Rouvinen, Juha
    [J]. JOURNAL OF STRUCTURAL BIOLOGY, 2011, 174 (01) : 156 - 163
  • [28] The crystal structure of acidic β-galactosidase from Aspergillus oryzae
    Maksimainen, Mirko M.
    Lampio, Anja
    Mertanen, Mirka
    Turunen, Ossi
    Rouvinen, Juha
    [J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2013, 60 : 109 - 115
  • [29] Lactose hydrolysis and formation of galactooligosaccharides by a novel immobilized β-galactosidase from the thermophilic fungus Talaromyces thermophilus
    Nakkharat, Phimchanok
    Haltrich, Dietmar
    [J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2006, 129 (1-3) : 215 - 225
  • [30] Properties of whey proteins obtained from different whey streams
    Nishanthi, Manjula
    Vasiljevic, Todor
    Chandrapala, Jayani
    [J]. INTERNATIONAL DAIRY JOURNAL, 2017, 66 : 76 - 83