Keratin degradation by Fervidobacterium pennavorans, a novel thermophilic anaerobic species of the order Thermotogales

被引:173
作者
Friedrich, AB [1 ]
Antranikian, G [1 ]
机构
[1] TECH UNIV HAMBURG,DEPT BIOTECHNOL,D-21071 HAMBURG,GERMANY
关键词
D O I
10.1128/AEM.62.8.2875-2882.1996
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
From a hot spring of the Azores islands a never thermophilic bacterium belonging to the Thermotogales order was isolated. This strain, which grows optimally at 70 degrees C and pH 6.5, is the first known extreme thermophile that is able to degrade native feathers at high temperatures. The enzyme system converts feather meal to amino acids and peptides. On the basis of physiological, morphological, and 16S rDNA studies the new isolate was found to be a member of the Thermotogales order and was identified as Fervidobacterium pennavorans, The strain was highly related to Fervidobacterium islandicum and Fervidobacterium pullulanolyticum. The cell-bound keratinolytic enzyme system was purified 32-fold by detergent treatment with CHAPS (3-[(3-cholamidopropyl)dimethyl-ammonio]-1-propanesulfonate) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme was characterized as a serine protease with a molecular mass of 130 kDa and an isoelectric point of 3.8. Optimal activity was measured at 80 degrees C and pH 10.0. Furthermore, 19 anaerobic thermophilic archaea and bacteria belonging to the orders Thermococcales, Thermoproteales, Thermotogales, and Clostridiales (growth temperatures between 60 and 105 degrees C) were tested for their abilities to grow on feathers and produce heat-stable keratinolytic enzymes, None of the tested extremophilic microorganisms was able to attack the substrate in a native form.
引用
收藏
页码:2875 / 2882
页数:8
相关论文
共 70 条
[1]   ISOLATION OF A THERMOSTABLE DEBRANCHING ENZYME (PULLULANASE) OF INDUSTRIAL RELEVANCE FROM A NEW FERVIDOBACTERIUM [J].
ANTRANIKIAN, G ;
KOCH, R .
CHEMIE INGENIEUR TECHNIK, 1992, 64 (06) :548-550
[2]   PURIFICATION AND CHARACTERIZATION OF MAJOR EXTRACELLULAR PROTEINASES FROM TRICHOPHYTON-RUBRUM [J].
ASAHI, M ;
LINDQUIST, R ;
FUKUYAMA, K ;
APODACA, G ;
EPSTEIN, WL ;
MCKERROW, JH .
BIOCHEMICAL JOURNAL, 1985, 232 (01) :139-144
[3]   METHANOGENS - RE-EVALUATION OF A UNIQUE BIOLOGICAL GROUP [J].
BALCH, WE ;
FOX, GE ;
MAGRUM, LJ ;
WOESE, CR ;
WOLFE, RS .
MICROBIOLOGICAL REVIEWS, 1979, 43 (02) :260-296
[4]   EFFECT OF STREPTOMYCIN AND NEAMINE ON STRUCTURE OF CHLOROPLAST AND MITOCHONDRIA IN CHLAMYDOMONAS-REINHARDII [J].
BEHN, W ;
ARNOLD, CG .
PROTOPLASMA, 1974, 82 (1-2) :77-89
[5]  
BELKIN S, 1986, APPL ENVIRON MICROB, V150, P477
[6]   IMPROVED SILVER STAINING OF PLANT-PROTEINS, RNA AND DNA IN POLYACRYLAMIDE GELS [J].
BLUM, H ;
BEIER, H ;
GROSS, HJ .
ELECTROPHORESIS, 1987, 8 (02) :93-99
[7]   CHARACTERIZATION OF SODIUM DODECYL SULFATE-RESISTANT PROTEOLYTIC ACTIVITY IN THE HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS-FURIOSUS [J].
BLUMENTALS, II ;
ROBINSON, AS ;
KELLY, RM .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1990, 56 (07) :1992-1998
[8]  
BOCKLE B, 1995, APPL ENVIRON MICROB, V61, P3705
[9]   Universal buffer soluttons and the association constant of veronal [J].
Britton, HTS ;
Robinson, RA .
JOURNAL OF THE CHEMICAL SOCIETY, 1931, :1456-1462
[10]   RAPID METHOD FOR BASE RATIO DETERMINATION OF BACTERIAL DNA [J].
CASHION, P ;
HOLDERFRANKLIN, MA ;
MCCULLY, J ;
FRANKLIN, M .
ANALYTICAL BIOCHEMISTRY, 1977, 81 (02) :461-466