Partial Purification and Computational Characterization Of L-asparaginase From Green Chillies in The Sudan

Abstract

Capsicum annum L

(Green chillies

)

has

several applications in food and pharmaceutical

s

. In the

food industry,

chilies are used for flavoring,

seasoning and appetizing purposes.

Green

chillies

contain appreciable amount of

L

-

asparaginase.

L

-

asparaginases are enzymes that catalyze the hydrolysis of L

-

asparagine to L

-

aspartate and

ammonia

.

U

sing amino acid sequences

and bioc

hemical properties as criteria;

enzymes w

ith

asparaginase activity was divided into several

families

including bacterial

and plant

-

type

asparagin

ases. The bacterial

-

type enzyme from

Ecoli

was clinically used to treat

patients

suffering from aspar

agines

–

dependent leukemias and lymphomas.

Experimental study was designed to extract and purify l

-

asparaginase enzyme from fruits of

green chillies plant

(Capsicum

annum

) in S

udan and then the enzyme activity in full set

condition

was

determine

d. Bioinfo

rmatics

tools

was used to

determine

the 3D structure of

enzyme

and

protein

sequence. Moreover, multiple alignments for sequence and structure

between en

zyme protein from plant sources

,

bacterial

sources

,

human

sources and phylogenetic

tree was performed by using different softwares.

As the result of the study Green

chillie

s contain appreciable amount of

L

-

asparaginase

with high

enzyme activity 111.6u/ml and specific activity 12.15 u/mg, optimum pH8.5 and optim

um

temperature 37C°

Computational analysis of plant

L

-

asparaginase

(Gossypium raimondii

)

showed high degree of

similarity to human

L

-

asparaginase

, and some differences from bacterial enzyme(

E.coli

).