Effect of laundry detergent formulation on the performance of alkaline phytoproteases

被引:8
作者
Barberis, Sonia [1 ]
Quiroga, Evelina [2 ]
Barcia, Cristina [1 ]
Liggieri, Constanza [3 ]
机构
[1] Univ Nacl San Luis, Inst Fis Aplicada, Lab Bromatol, San Luis, Argentina
[2] Univ Nacl San Luis, Inst Fis Aplicada, Lab Membranas & Biomat, San Luis, Argentina
[3] Univ Nacl La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, Lab Invest Prot Vegetales, La Plata, Buenos Aires, Argentina
关键词
asclepain; araujiain; detergents formulations; alkaline plant proteases; PEPTIDE-SYNTHESIS; FUNASTRUM-CLAUSUM; UNRIPE FRUITS; PROTEASE; LATEX; PURIFICATION;
D O I
10.2225/vol16-issue3-fulltext-1
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
Background: Proteases constitute the largest product segment in the global industrial enzymes market; they are used in food, pharmaceutical, leather, textile, wood and detergent industries. Alkaline proteases improve the cleaning efficiency of detergents and represent one of the most successful applications of modern industrial biotechnology. The aim of this work was to study the performance of two alkaline phytoproteases, araujiain (Araujia hortorum Fourn.) and asclepain (Asclepias curassavica L.), for their potential application as additive in laundry detergent formulations. Results: The effect of pure non-ionic and ionic surfactants on proteolytic activity of araujiain and asclepain was analyzed measuring the remaining activity after 1 hr of incubation of those enzymes in aqueous solutions of surfactants at different concentrations (0.1, 0.4 and 1% v/v) and temperatures (25, 40 and 60 degrees C). Besides, the compatibility of the enzymes with six commercial laundry detergents was also studied measuring the remaining proteolytic activity at 37 degrees C after 1 hr. Commercial detergent components influenced in different ways on araujiain and asclepain, in spite of the similar behaviour of the two enzymes in buffer. In commercial detergent solutions, araujiain expressed between 60% and 140% of its remaining proteolytic activity in buffer (pH 8.5) at 37 degrees C after 1 hr, while asclepain, was practically inactivate in most of them at the same conditions. Conclusions: Proteolytic extract of Araujia hortorum fulfilled all the requirements for its application as additive for laundry detergents: high stability in a broad temperature range (25-70 degrees C), high activity in alkaline pH (7.5-9.5) and very good compatibility with the commercial detergent additives. Nevertheless, in spite of its high stability and activity in buffer, the proteolytic extract of Asclepias curassavica did not show the same performance than araujiain.
引用
收藏
页数:8
相关论文
共 35 条
[1]   Production of alkaline proteases by Botrytis cinerea using economic raw materials: Assay as biodetergent [J].
Abidi, Ferid ;
Limam, Ferid ;
Nejib, Marzouki M. .
PROCESS BIOCHEMISTRY, 2008, 43 (11) :1202-1208
[2]   Strategies towards the functionalization of subtilisin E from Bacillus subtilis for wool finishing applications [J].
Araujo, R. ;
Cavaco-Paulo, A. ;
Casal, M. .
ENGINEERING IN LIFE SCIENCES, 2008, 8 (03) :238-249
[3]  
Arunachalam C., 2009, INDIAN J SCI TECHNOL, V2, P29, DOI [10.17485/ijst/2009/v2i12.10, DOI 10.17485/IJST/2009/V2I12.10]
[4]   Thermostable alkaline protease from Bacillus brevis and its characterization as a laundry detergent additive [J].
Banerjee, UC ;
Sani, RK ;
Azmi, W ;
Soni, R .
PROCESS BIOCHEMISTRY, 1999, 35 (1-2) :213-219
[5]   Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease brachystephana isolated from Morrenia (Asclepiadaceae) [J].
Barberis, SB ;
Quiroga, E ;
Arribére, MC ;
Priolo, N .
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2002, 17 (01) :39-47
[6]  
Barberis Sonia, 2008, P253, DOI 10.1007/978-1-4020-8361-7_6
[7]  
BARCIA C., 2010, DETERGENTS TYPES COM, P143
[8]  
Barcia C, 2009, BIOTECH AGR IND MED, P293
[9]  
DONLON J, 2007, IND ENZYMES STRUCTUR, P196
[10]  
Doran PM, 2002, BOOK SOIL P, P143