Screening and identification of a Bacillus amyloliquefaciens strain for aqueous enzymatic extraction of medium-chain triglycerides

Cheng Zeng, Rongbin Zhao, Xuefang Wen, Ping Yu, Zheling Zeng, Shuguang Deng, Deming Gong

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A strain with a high yield of neutral proteinase and low yield of lipase, resistance to medium chain fatty acid triglycerides is the key to increasing yield and quality of Cinnamomum camphora seed kernel oil (CCSKO) with aqueous enzymatic extraction technology. A bacterial strain, NCU116 isolated from the waste residue produced in CCSKO production through primary screening with plate and secondary screening with shake-flask fermentation. It was found to be suitable for the extraction of CCSKO or other medium-chain triglycerides by using the extraction technology. Its activity of neutral proteinase was 4536.5 U/mL, and only 0.088 U/mL for lipase production. The strain was identified as Bacillus amyloliquefaciens by morphological, physiological, biochemical and 16S rDNA molecular identification. The extracellular enzymes produced by NCU116 included neutral proteinase, pectinase, glucoamylase, cellulase, amylase and lipase. The neutral proteinase had the maximum activity at 50 °C, but was unstable. Its optimum temperature and pH value were approximately 40 °C and 7.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 45 °C, and was activated by Ca2+, Zn2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 45–50 °C and 6.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Cu2+, Fe2+, Mn2+ and Ca2+. Its optimum temperatures and pH value were 35–40 °C and 7.0 respectively. The cellulase had the maximum activity at 35 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 30–40 °C and 7.0 respectively.

Original languageEnglish (US)
Pages (from-to)24-32
Number of pages9
JournalFood Control
Volume78
DOIs
StatePublished - Aug 1 2017

Fingerprint

Bacillus amyloliquefaciens
medium chain triacylglycerols
Cinnamomum camphora
Triglycerides
Peptide Hydrolases
screening
proteinases
Lipase
Glucan 1,4-alpha-Glucosidase
Polygalacturonase
seeds
Seeds
Oils
Temperature
Cellulase
glucan 1,4-alpha-glucosidase
water
polygalacturonase
calcium
endo-1,4-beta-glucanase

Keywords

  • Bacillus amyloliquefaciens
  • Enzymatic properties
  • Identification
  • Screening

ASJC Scopus subject areas

  • Biotechnology
  • Food Science

Cite this

Screening and identification of a Bacillus amyloliquefaciens strain for aqueous enzymatic extraction of medium-chain triglycerides. / Zeng, Cheng; Zhao, Rongbin; Wen, Xuefang; Yu, Ping; Zeng, Zheling; Deng, Shuguang; Gong, Deming.

In: Food Control, Vol. 78, 01.08.2017, p. 24-32.

Research output: Contribution to journalArticle

Zeng, Cheng ; Zhao, Rongbin ; Wen, Xuefang ; Yu, Ping ; Zeng, Zheling ; Deng, Shuguang ; Gong, Deming. / Screening and identification of a Bacillus amyloliquefaciens strain for aqueous enzymatic extraction of medium-chain triglycerides. In: Food Control. 2017 ; Vol. 78. pp. 24-32.
@article{24457737a3d1482d859ac5f6ac080850,
title = "Screening and identification of a Bacillus amyloliquefaciens strain for aqueous enzymatic extraction of medium-chain triglycerides",
abstract = "A strain with a high yield of neutral proteinase and low yield of lipase, resistance to medium chain fatty acid triglycerides is the key to increasing yield and quality of Cinnamomum camphora seed kernel oil (CCSKO) with aqueous enzymatic extraction technology. A bacterial strain, NCU116 isolated from the waste residue produced in CCSKO production through primary screening with plate and secondary screening with shake-flask fermentation. It was found to be suitable for the extraction of CCSKO or other medium-chain triglycerides by using the extraction technology. Its activity of neutral proteinase was 4536.5 U/mL, and only 0.088 U/mL for lipase production. The strain was identified as Bacillus amyloliquefaciens by morphological, physiological, biochemical and 16S rDNA molecular identification. The extracellular enzymes produced by NCU116 included neutral proteinase, pectinase, glucoamylase, cellulase, amylase and lipase. The neutral proteinase had the maximum activity at 50 °C, but was unstable. Its optimum temperature and pH value were approximately 40 °C and 7.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 45 °C, and was activated by Ca2+, Zn2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 45–50 °C and 6.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Cu2+, Fe2+, Mn2+ and Ca2+. Its optimum temperatures and pH value were 35–40 °C and 7.0 respectively. The cellulase had the maximum activity at 35 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 30–40 °C and 7.0 respectively.",
keywords = "Bacillus amyloliquefaciens, Enzymatic properties, Identification, Screening",
author = "Cheng Zeng and Rongbin Zhao and Xuefang Wen and Ping Yu and Zheling Zeng and Shuguang Deng and Deming Gong",
year = "2017",
month = "8",
day = "1",
doi = "10.1016/j.foodcont.2017.02.031",
language = "English (US)",
volume = "78",
pages = "24--32",
journal = "Food Control",
issn = "0956-7135",
publisher = "Elsevier BV",

}

TY - JOUR

T1 - Screening and identification of a Bacillus amyloliquefaciens strain for aqueous enzymatic extraction of medium-chain triglycerides

AU - Zeng, Cheng

AU - Zhao, Rongbin

AU - Wen, Xuefang

AU - Yu, Ping

AU - Zeng, Zheling

AU - Deng, Shuguang

AU - Gong, Deming

PY - 2017/8/1

Y1 - 2017/8/1

N2 - A strain with a high yield of neutral proteinase and low yield of lipase, resistance to medium chain fatty acid triglycerides is the key to increasing yield and quality of Cinnamomum camphora seed kernel oil (CCSKO) with aqueous enzymatic extraction technology. A bacterial strain, NCU116 isolated from the waste residue produced in CCSKO production through primary screening with plate and secondary screening with shake-flask fermentation. It was found to be suitable for the extraction of CCSKO or other medium-chain triglycerides by using the extraction technology. Its activity of neutral proteinase was 4536.5 U/mL, and only 0.088 U/mL for lipase production. The strain was identified as Bacillus amyloliquefaciens by morphological, physiological, biochemical and 16S rDNA molecular identification. The extracellular enzymes produced by NCU116 included neutral proteinase, pectinase, glucoamylase, cellulase, amylase and lipase. The neutral proteinase had the maximum activity at 50 °C, but was unstable. Its optimum temperature and pH value were approximately 40 °C and 7.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 45 °C, and was activated by Ca2+, Zn2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 45–50 °C and 6.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Cu2+, Fe2+, Mn2+ and Ca2+. Its optimum temperatures and pH value were 35–40 °C and 7.0 respectively. The cellulase had the maximum activity at 35 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 30–40 °C and 7.0 respectively.

AB - A strain with a high yield of neutral proteinase and low yield of lipase, resistance to medium chain fatty acid triglycerides is the key to increasing yield and quality of Cinnamomum camphora seed kernel oil (CCSKO) with aqueous enzymatic extraction technology. A bacterial strain, NCU116 isolated from the waste residue produced in CCSKO production through primary screening with plate and secondary screening with shake-flask fermentation. It was found to be suitable for the extraction of CCSKO or other medium-chain triglycerides by using the extraction technology. Its activity of neutral proteinase was 4536.5 U/mL, and only 0.088 U/mL for lipase production. The strain was identified as Bacillus amyloliquefaciens by morphological, physiological, biochemical and 16S rDNA molecular identification. The extracellular enzymes produced by NCU116 included neutral proteinase, pectinase, glucoamylase, cellulase, amylase and lipase. The neutral proteinase had the maximum activity at 50 °C, but was unstable. Its optimum temperature and pH value were approximately 40 °C and 7.0 respectively. Mn2+ was an activator of neutral proteinase. The glucoamylase had the maximum activity at 45 °C, and was activated by Ca2+, Zn2+, Fe3+ and Mn2+. Its optimum temperatures and pH value were 45–50 °C and 6.0 respectively. The pectinase had the maximum activity at 40 °C, and was activated by Cu2+, Fe2+, Mn2+ and Ca2+. Its optimum temperatures and pH value were 35–40 °C and 7.0 respectively. The cellulase had the maximum activity at 35 °C, and was activated by Ca2+ and Mn2+. Its optimum temperatures and pH value were 30–40 °C and 7.0 respectively.

KW - Bacillus amyloliquefaciens

KW - Enzymatic properties

KW - Identification

KW - Screening

UR - http://www.scopus.com/inward/record.url?scp=85013680635&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85013680635&partnerID=8YFLogxK

U2 - 10.1016/j.foodcont.2017.02.031

DO - 10.1016/j.foodcont.2017.02.031

M3 - Article

AN - SCOPUS:85013680635

VL - 78

SP - 24

EP - 32

JO - Food Control

JF - Food Control

SN - 0956-7135

ER -