[Federal Register Volume 63, Number 85 (Monday, May 4, 1998)]
[Rules and Regulations]
[Pages 24416-24419]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 98-11681]
[[Page 24416]]
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DEPARTMENT OF HEALTH AND HUMAN SERVICES
Food and Drug Administration
21 CFR Part 184
[Docket No. 90G-0412]
Lipase Enzyme Preparation From Rhizopus Niveus; Affirmation of
GRAS Status as a Direct Food Ingredient
AGENCY: Food and Drug Administration, HHS.
ACTION: Final rule.
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SUMMARY: The Food and Drug Administration (FDA) is amending its
regulations to affirm that lipase enzyme preparation derived from
Rhizopus niveus is generally recognized as safe (GRAS) for use as a
direct human food ingredient. This action is in response to a petition
submitted by Fuji Oil Co., Ltd.
DATES: The regulation is effective May 4, 1998. The Director of the
Office of the Federal Register approves the incorporation by reference
in accordance with 5 U.S.C. 552(a) and 1 CFR part 51 of a certain
publication listed in Sec. 184.1420 (21 CFR 184.1420), effective May 4,
1998.
FOR FURTHER INFORMATION CONTACT: Linda S. Kahl, Center for Food Safety
and Applied Nutrition (HFS-206), Food and Drug Administration, 200 C
St. SW., Washington, DC 20204, 202-418-3101.
SUPPLEMENTARY INFORMATION:
I. Background
In accordance with the procedures described in 21 CFR 170.35, Fuji
Oil Co., Ltd., submitted a petition (GRASP 7G0330) requesting that
lipase-protease enzyme preparation from R. niveus be affirmed as GRAS
for use as a direct human food ingredient. FDA published a notice of
filing of this petition in the Federal Register of June 18, 1992 (57 FR
27256), and gave interested persons an opportunity to submit comments
to the Dockets Management Branch (HFA-305), Food and Drug
Administration, 12420 Parklawn Dr., rm. 1-23, Rockville, MD 20857. FDA
received no comments in response to the filing notice.
Although the petitioner proposed that the subject enzyme
preparation be called by the common or usual name ``lipase-protease,''
the proposed use of the enzyme preparation is solely for its lipase
activity. The GRAS exemption described in section 201(s) of the Federal
Food, Drug, and Cosmetic Act (21 U.S.C. 321(s)) specifies that a GRAS
substance must be generally recognized as safe ``under the conditions
of its intended use.'' Thus, affirmation of GRAS status pertains to the
particular use of a substance. Accordingly, FDA considers the enzyme
preparation that is the subject of this document to be ``lipase enzyme
preparation.'' To avoid confusion between lipase, the enzyme, and the
lipase-containing enzyme preparation, which contains lipase as its
characterizing enzyme activity, but which also contains diatomaceous
earth as a carrier and may contain other enzyme activities and
impurities, this document will henceforth use the terms ``lipase'' to
refer to the enzyme and ``lipase enzyme preparation'' to refer to the
fermentation-derived lipase enzyme preparation, including the carrier
diatomaceous earth.
II. Standards for GRAS Affirmation
Under Sec. 170.30 (21 CFR 170.30), general recognition of safety
may be based only on the views of experts qualified by scientific
training and experience to evaluate the safety of substances directly
or indirectly added to food. The basis of such views may be either
scientific procedures or, in the case of a substance used in food prior
to January 1, 1958, experience based on common use in food. General
recognition of safety based upon scientific procedures requires the
same quantity and quality of scientific evidence as is required to
obtain approval of a food additive regulation and ordinarily is based
upon published studies, which may be corroborated by unpublished
studies and other data and information (Sec. 170.30(b)). General
recognition of safety through experience based on common use in food
prior to January 1, 1958, may be determined without the quantity or
quality of scientific procedures required for approval of a food
additive regulation, and ordinarily is based upon generally available
data and information.
FDA has evaluated Fuji Oil Co., Ltd.'s petition on the basis of
scientific procedures to establish that the use of lipase enzyme
preparation as an enzymatic catalyst for the interesterification of
fats and oils is GRAS. In evaluating the petition, FDA considered: (1)
Published and unpublished data and information relating to the identity
and function of the enzyme component (i.e., lipase) (Refs. 1 through
5); (2) published and unpublished data and information relating to the
production organism (Ref. 6); and (3) published and unpublished
information, methods, and principles relating to the methods and
processing aids used in the manufacture of the enzyme preparation
(Refs. 4 and 7 through 10).
III. Safety Evaluation
A. Introduction
Commercial enzyme preparations that are used in food processing
typically are not chemically pure but contain, in addition to the
enzyme component, other components that derive from the production
organism and the fermentation media, residual amounts of processing
aids, and substances used as stabilizers, preservatives or diluents.
Issues relevant to a safety evaluation of the enzyme preparation
therefore include the safety of the enzyme component, the safety of the
enzyme source, and the safety of processing aids and other substances
added during the manufacturing process. As with all substances added to
food, a safety evaluation of an enzyme preparation also includes
consideration of dietary exposure to that preparation.
B. The Enzyme Component
Triglycerides are fats or oils comprised of fatty acids linked by
ester bonds to each of the three hydroxyl groups of glycerol.
Triacylglycerol lipases catalyze the hydrolysis of these ester bonds
and can be grouped according to their specificity. The lipase produced
by Geotrichum candidium, for example, preferentially cleaves
triglycerides containing long-chain fatty acids with a cis double bond
in the 9-position, but such specificity for the hydrolysis of esters
containing a particular type of fatty acid is unusual. Several other
lipases (e.g., the lipase derived from Candida cylindracae) are
nonspecific with respect to either the chemical structure of the fatty
acid moiety, or the position of the ester bond, that is hydrolyzed;
these lipases catalyze the complete breakdown of triglycerides into
glycerol and free fatty acids, and the mono- and diglycerides that are
intermediates in the reaction do not normally accumulate (Refs. 2 and
4).
The largest group of triacylglycerol lipases exhibits specificity
with respect to the position of the ester bond that is cleaved, i.e.,
only bonds at the 1- or 3-position of the glycerol component are
hydrolyzed. Most of the lipases that are commonly used in food
processing (e.g., animal lipase, esterase-lipase from Mucor miehei, and
lipases derived from Aspergillus niger, M. javanicus, and R. delemar),
including the R. niveus-derived lipase that is the subject of this
document, belong to this group (EC No. 3.1.1.3; CAS Reg. No. 9001-62-1)
(Refs. 2, 4, and 11).
Although the petitioner did not address the detailed molecular
structure of lipase from R. niveus, most lipases that have been
characterized at the
[[Page 24417]]
molecular level are glycoproteins that contain between 2 and 15 percent
carbohydrates, with mannose as the major glycoside (Ref. 4). Lipases
from animal and microbial sources have a long history of use in food.
Animal lipase (21 CFR 184.1415) is affirmed as GRAS based on its common
use in food prior to January 1, 1958. Esterase-lipase from the fungus
M. miehei (21 CFR 173.140) is approved for use as a food additive.
These enzymes are commonly used to enhance flavor production in cheese
and in butterfat (Refs. 1, 12, and 13). In addition, lipases from
animal sources (e.g., bovine stomach and hog or porcine pancreas) and
microbial sources (including R. arrhizus, R. delemar, and R. niveus)
have been listed in the Codex Alimentarius Commission ``Inventory of
Processing Aids'' (Ref. 14).
The reaction product of the R. niveus-derived lipase is a mixture
of mono- and diglycerides and free fatty acids (Refs. 2 through 5). The
reaction catalyzed by this lipase is reversible and, therefore, under
appropriate conditions the enzyme can catalyze the synthesis of
triglycerides from a mixture of glycerides and free fatty acids. When
this combination of hydrolysis and synthesis occurs within a mixture of
triglycerides, or within a mixture of triglycerides and fatty acid
esters, the reaction products are triglycerides that have been
interesterified, i.e., triglycerides in which the fatty acid components
have been exchanged between triglyceride molecules or between
triglyceride molecules and fatty acid esters (Refs. 1 through 5). For
example, the GRAS food ingredient ``cocoa butter substitute primarily
from palm oil'' may be manufactured by the lipase-catalyzed
interesterification of partially saturated palm oil-derived
triglycerides with the fatty acid ester ethyl stearate (21 CFR
184.1259).
Interesterification also can be achieved through the use of
chemical catalysts such as sodium methylate. Such chemical catalysis
results in random interesterification, in which fatty acid interchange
occurs at all three positions on the glycerol backbone. In contrast,
enzymatic catalysis with a lipase, such as the lipase that is the
subject of this document, results in selective interesterification at
the 1- and 3-positions only. Random interesterification is used
commercially in the manufacture of margarines and shortenings, but
lipase-catalyzed selective interesterification, which allows an
unsaturated fatty acid to remain at the 2-position, is important in the
manufacture of fats and oils used in confectionery, such as cocoa
butter substitute primarily from palm oil (Refs. 2 through 4). The
petitioner stated that one of the primary uses of R. niveus-derived
lipase enzyme preparation would be in the manufacture of cocoa butter
substitute primarily from palm oil.
In general, issues relevant to a safety evaluation of proteins such
as the enzyme component of an enzyme preparation are potential toxicity
and allergenicity (Ref. 15). Pariza and Foster (Ref. 15) note that very
few toxic agents have enzymatic properties, and those that do (e.g.,
diphtheria toxin and certain enzymes in the venom of poisonous snakes)
catalyze unusual reactions that are not related to the reactions
catalyzed by enzymes that are commonly used in food processing, such as
the lipase that is the subject of this document. Further, the agency
has recently noted, in the context of guidance to industry regarding
the safety assessment of new plant varieties, that enzymes themselves
do not generally raise safety concerns (57 FR 22984 at 23005, May 29,
1992). Exceptions include enzymes that produce substances that are not
ordinarily digested and metabolized, or that produce toxic substances.
The catalytic activities of the lipase that is the subject of this
document are well known. As already discussed, lipase catalyzes two
related reactions: (1) The splitting of commonly consumed triglycerides
into smaller components, i.e., fatty acids and mono- and diglycerides;
and (2) the synthesis of triglycerides from fatty acids and mono- and
diglycerides. The reaction products (i.e., fatty acids, mono- and
diglycerides, and triglycerides) from both of these reactions are
readily metabolized by the human body and do not have toxic properties
(Ref. 16).
The agency is not aware of any reports of allergic reactions
associated with the ingestion of enzymes derived from Rhizopus species.
There have been, however, some reports of allergies and primary
irritations from skin contact with enzymes or from inhalation of dust
from concentrated enzymes (e.g., proteases used in the manufacture of
laundry detergents) (Refs. 17 through 19). These reports relate
primarily to workers in production plants (Ref. 18) and are not
relevant to an evaluation of the safety of ingestion of such enzymes in
food. Moreover, Pariza and Foster (Ref. 15) note that there are no
confirmed reports of primary irritations in consumers caused by
residues of food processing enzymes in food.
FDA concludes that generally available and accepted data and
information establish that the use of lipase in food raises no toxicity
or allergenicity concerns. FDA also concludes that generally available
and accepted data and information establish that the lipase that is the
subject of this document is capable of achieving its intended technical
effect. Finally, FDA concludes that generally available and accepted
data and information establish that the lipase that is the subject of
this document is similar in function to other lipases that are used in
food processing to catalyze the hydrolysis of ester bonds at the 1- or
3-position of the glycerol component of a triglyceride.
C. Enzyme Source, Manufacturing Methods, and Processing Aids
The source of the lipase that is the subject of this document is
the fungus R. niveus. Fungally-derived enzyme preparations used in food
processing are usually not chemically pure but contain, in addition to
the enzyme component, other components that derive from the production
organism and the fermentation media, residual amounts of processing
aids, and substances used as stabilizers, preservatives or diluents.
The petitioned enzyme preparation meets the general requirements and
additional requirements for enzyme preparations in the monograph on
Enzyme Preparations in the Food Chemicals Codex, 4th ed. (Ref. 20).
When the R. niveus-derived lipase enzyme preparation is produced in
accordance with current good manufacturing practice (CGMP), it is
produced using processing aids that are substances that are acceptable
for general use in foods and under culture conditions that ensure a
controlled fermentation, thus preventing the introduction of extraneous
microorganisms that could be the source of toxic materials and other
toxic substances (Ref. 20).
The lipase enzyme preparation is produced in a multistage process
by controlled fermentation\1\ using a pure culture of the fungus R.
niveus followed by isolation of the enzyme-containing fraction. Prior
to its use in the interesterification of fats and oils, the enzyme-
containing fraction is adsorbed onto diatomaceous earth as a carrier.
These methods are based upon generally available and accepted methods
used for fermentation, for processing fermentation-derived enzyme-
containing fractions, and for immobilizing an enzyme-containing
fraction on an insoluble carrier (Refs. 4 and 7 through 10).
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\1\ The stage of the manufacturing process in which the enzyme
is being produced by an actively growing culture of microorganisms
is referred to as fermentation.
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[[Page 24418]]
In the initial stage of the fermentation process, the seed cultures
of R. niveus are checked for purity and classification after growth on
a potato-agar medium. The production cultures are suspended in sterile
water and added to a previously autoclaved wheat bran culture medium.
After growth for 28 to 32 hours, the broth is checked for quality and
added to large batch-fermentors containing sterilized growth medium
(semisolid wheat bran). The culture is monitored until the water
content and pH value of the resulting malt, which is referred to as the
``koji,'' reach standard requirements.
A cell-free extract of the enzymes that are components of the
fermentation mixture is prepared by sprinkling and steeping the koji
with cold water, filtering the extracted koji through a filter press
and a fine filtration apparatus, and precipitating the enzymes that are
present in the resulting filtrate with ethanol. After decanting the
supernatant and centrifuging the remaining slurry, the sediment
containing the extracted enzymes is collected and dried overnight in a
vacuum-dryer at 40 to 45 deg.C. The dried powder is ground, sized, and
mixed before storing at room temperature. The finished product is
adjusted to a standard activity by mixing the enzyme powder with
dextrin as an excipient. The standardized enzyme powder is adsorbed
onto diatomaceous earth carrier prior to its use in the
interesterification of fats or oils. The petitioner provided a
published scientific review article that discusses this immobilization
technique with respect to use of lipase enzyme preparations (Ref. 4).
The production strain of R. niveus that is the source of the lipase
enzyme is nontoxigenic and nonpathogenic. The manufacturing methods
completely remove the organism from the enzyme-containing fraction
(Ref. 4). Moreover, the petitioner provided documentation, based upon
published methods for strain identification (Ref. 6), showing that the
production strain was taxonomically identical to the strain used for
the production of R. niveus-derived amyloglucosidase enzyme
preparation, which is approved for use as a secondary direct food
additive (21 CFR 173.110).
FDA concludes that the presence of added substances and impurities
that are derived from the enzyme source or that are introduced by
manufacturing does not present a basis for concern about the safety of
the lipase enzyme preparation.
D. Dietary Exposure
FDA considered the estimated dietary exposure to lipase enzyme
preparation for the proposed use as an enzymatic catalyst in the
interesterification of fats and oils (Refs. 21 through 23). The
predominant source of potential exposure to the total organic solids in
the enzyme preparation will be baked goods that use interesterified fat
at levels up to 30 percent. The petitioner stated that the standardized
enzyme powder is adsorbed onto diatomaceous earth carrier prior to its
use in the interesterification of fats or oils, so that it can be
removed from the modified triglyceride following the enzyme-catalyzed
interesterification. Because the adsorbed enzyme preparation is removed
from the interesterified product following catalysis, no detectable
enzyme remains in the interesterified product.
FDA concludes that dietary exposure to the lipase enzyme
preparation is negligible and therefore does not present a basis for
concern about use of the lipase enzyme preparation.
IV. Specifications
The agency finds that, because the potential impurities in the
lipase enzyme preparation that may originate from the source or
manufacturing process do not raise any basis for concern about the safe
use of the preparation, the general requirements and additional
requirements for enzyme preparations in the monograph on Enzyme
Preparations in the Food Chemicals Codex, 4th ed. (1996), which are
being incorporated by reference in accordance with 5 U.S.C. 552(a) and
1 CFR part 51, are adequate as minimum criteria for food-grade lipase
enzyme preparation. Lipase assay can be performed using a method
entitled ``Lipase Activity'' (Ref. 24) or by using any appropriate
validated method.
V. Conclusions
The agency has evaluated all available information and finds, based
upon the published information about the identity and function of
lipase, that the enzyme component of lipase enzyme preparation will
achieve its intended technical effect and raises no toxicity or
allergenicity concerns. In addition, the agency finds, based upon the
published information about the identity and function of lipase, that
the enzyme component of the lipase enzyme preparation is similar in
function to other lipases that are used in food processing to catalyze
the hydrolysis of ester bonds at the 1- or 3-position of the glycerol
component of a triglyceride. The agency further finds, based upon
generally available and accepted information, that when the lipase
enzyme preparation is manufactured in accordance with Sec. 184.1420,
the source, R. niveus, and the manufacturing process will not introduce
impurities into the preparation that may render its use unsafe.
Finally, the agency finds that dietary exposure to the lipase enzyme
preparation from the petitioned use does not present a basis for
concern about use of the lipase enzyme preparation. Therefore, the
agency concludes, based upon the evaluation of published data and
information, corroborated by unpublished data and information, and
based upon scientific procedures (Sec. 170.30(b)), that the lipase
enzyme preparation described in the regulation set out below is GRAS
for use as an enzymatic catalyst in the interesterification of fats and
oils.
VI. Environmental Considerations
The agency has carefully considered the potential environmental
effects of this action. FDA has concluded that the action will not have
a significant impact on the human environment, and that an
environmental impact statement is not required. The agency's finding of
no significant impact and the evidence supporting that finding,
contained in an environmental assessment, may be seen in the Dockets
Management Branch (address above) between 9 a.m. and 4 p.m., Monday
through Friday.
VII. Analysis For Executive Order 12866
FDA has examined the impacts of this final rule under Executive
Order 12866. Executive Order 12866 directs Federal agencies to assess
the costs and benefits of available regulatory alternatives and, when
regulation is necessary, to select regulatory approaches that maximize
net benefits (including potential economic, environmental, public
health and safety effects; distributive impacts; and equity). According
to Executive Order 12866, a regulatory action is significant if it
meets any one of a number of specified conditions, including having an
annual effect on the economy of $100 million, adversely affecting in a
material way a sector of the economy, competition, or jobs, or if it
raises novel legal or policy issues. FDA finds that this final rule is
not a significant regulatory action as defined by Executive Order
12866. In addition, the agency has determined that this final rule is
not a major rule for the purpose of Congressional review.
The primary benefit of this action is to remove uncertainty about
the regulatory status of the petitioned
[[Page 24419]]
substance. No compliance costs are associated with this final rule
because no new activity is required and no current or future activity
is prohibited by this rule.
VIII. Regulatory Flexibility Analysis
FDA has examined the impacts of this final rule under the
Regulatory Flexibility Act. The Regulatory Flexibility Act (5 U.S.C.
601-612) requires Federal agencies to consider alternatives that would
minimize the economic impact of their regulations on small entities. No
compliance costs are associated with this final rule because no new
activity is required and no current or future activity is prohibited.
Accordingly, under the Regulatory Flexibility Act (5 U.S.C. 605(b)),
the agency certifies that this final rule will not have a significant
economic impact on a substantial number of small entities.
IX. References
The following references have been placed on display in the
Dockets Management Branch (address above) and may be seen by interested
persons between 9 a.m. and 4 p.m., Monday through Friday.
1. Scott, D., ``Enzymes, Industrial,'' Encyclopedia of Chemical
Technology, edited by Mark, H. F. et al., John Wiley and Sons, New
York, 3d ed., 9:173-224, 1978.
2. MacRae, A. R., ``Lipase-Catalyzed Interesterification of Fats
and Oils,'' Journal of the American Oil Chemists Society, 60:291-
294, 1983.
3. Ratledge, C., ``Biotechnology as Applied to the Oils and Fats
Industry,'' Fette Seifen Anstrichmittel, 86:379-389, 1984.
4. MacRae, A. R., and R. C. Hammond, ``Present and Future
Applications of Lipases,'' Biotechnology and Genetic Engineering
Reviews, 3:193-217, 1985.
5. IUB, ``Enzyme Nomenclature 1992,'' Academic Press, New York,
p. 307, 1992.
6. Inui, T., Y. Takeda, and H. Iizuka, ``Taxonomical Studies on
Genus Rhizopus,'' Journal of General and Applied Microbiology, 11:1-
121, 1965.
7. Beckhorn, E. J., M. D. Labee, and L. A. Underkofler,
``Production and Use of Microbial Enzymes for Food Processing,''
Journal of Agricultural and Food Chemistry, 13:30-34, 1965.
8. Underkofler, L. A., R. R. Barton, and S. S. Rennet,
``Microbiological Process Report--Production of Microbial Enzymes
and Their Applications,'' Applied Microbiology, 6:212-221, 1958.
9. Chibata, Ichiro, ed., Immobilized Enzymes--Research and
Development, John Wiley and Sons, New York, 1978.
10. Chaplin, M. F., and C. Bucke, Enzyme Technology, Cambridge
University Press, New York, 1990.
11. Shahani, K. M., ``Lipases and Esterases,'' Enzymes in Food
Processing, edited by Reed, G., Academic Press, New York, 2d ed.,
pp. 208-214, 1975.
12. Reed, G., ``Industrial Enzymes-Now Speed Natural
Processes,'' Food Engineering, 24:105-109, 1952.
13. De Becze, G. I., ``Food Enzymes,'' Critical Reviews in Food
Technology, 1:479-518, 1970.
14. Codex Alimentarius, Joint FAO/WHO Food Standards Programme,
Food and Agriculture Organization of the United Nations/World Health
Organization, Rome, vol. 1, 2d ed., 1992.
15. Pariza, M. W., and E. M. Foster, ``Determining the Safety of
Enzymes Used in Food Processing,'' Journal of Food Protection,
46:453-468, 1983.
16. Shils, M. E., J. A. Olson and M. Shike, eds., Modern
Nutrition in Health and Disease, Lea & Febiger, Philadelphia, 8th
ed., pp. 51-57, 1994.
17. ``Evaluation of the Health Aspects of Papain as a Food
Ingredient,'' Select Committee on GRAS Substances, Washington, DC,
available through U.S. Department of Commerce, National Technical
Information Service, Order No. PB-274-174, 1977.
18. Fulwiler, R. D., ``Detergent Enzymes--An Industrial Hygiene
Challenge,'' American Industrial Hygiene Association Journal, 32:73-
81, 1971.
19. ``Enzyme-containing Laundering Compounds and Consumer
Health,'' National Research Council/National Academy of Sciences,
National Technical Information Service, Washington, DC, Order No.
PB-204-118, 1971.
20. Monograph on ``Enzyme Preparations,'' Food Chemicals Codex,
National Academy Press, Washington, DC, 4th ed., pp. 131 and 133-
134, 1996.
21. Memorandum dated October 21, 1988, from Food and Color
Additives Review Section, FDA, to Direct Additives Branch, FDA,
``Lipase/Protease Enzyme Preparation Derived from Rhizopus niveus.''
22. Memorandum dated March 8, 1989, from Food and Color
Additives Review Section, FDA, to Direct Additives Branch, FDA,
``Lipase-Protease Enzyme Preparation from Rhizopus niveus.''
23. Memorandum dated April 3, 1990, from Food and Color
Additives Review Section, FDA, to Direct Additives Branch, FDA,
``Lipase/Protease Enzyme Preparation from Rhizopus niveus.
Refinement of Estimated Daily Intake (EDI). Submission of 3-6-90.''
24. Monograph on ``Enzyme Preparations,'' Food Chemicals Codex,
National Academy Press, Washington, DC, 4th ed., p. 803, 1996.
List of Subjects in 21 CFR Part 184
Food additives, Incorporation by reference.
Therefore, under the Federal Food, Drug, and Cosmetic Act and under
authority delegated to the Commissioner of Food and Drugs, and
redelegated to the Director, Center for Food Safety and Applied
Nutrition, part 184 is amended as follows:
PART 184--DIRECT FOOD SUBSTANCES AFFIRMED AS GENERALLY RECOGNIZED
AS SAFE
1. The authority citation for 21 CFR part 184 continues to read as
follows:
Authority: 21 U.S.C. 321, 342, 348, 371.
2. Section 184.1420 is added to subpart B to read as follows:
Sec. 184.1420 Lipase enzyme preparation derived from Rhizopus niveus.
(a) Lipase enzyme preparation contains lipase enzyme (CAS Reg. No.
9001-62-1), which is obtained from the culture filtrate resulting from
a pure culture fermentation of a nonpathogenic and nontoxigenic strain
of Rhizopus niveus. The enzyme preparation also contains diatomaceous
earth as a carrier. The characterizing activity of the enzyme, which
catalyzes the interesterification of fats and oils at the 1- and 3-
positions of triglycerides, is triacylglycerol lipase (EC 3.1.1.3).
(b) The ingredient meets the general requirements and additional
requirements for enzyme preparations in the monograph on Enzyme
Preparations in the ``Food Chemicals Codex,'' 4th ed. (1996), pp. 133
and 134, which is incorporated by reference in accordance with 5 U.S.C.
552(a) and 1 CFR part 51. Copies are available from the National
Academy Press, 2101 Constitution Ave. NW., Washington, DC 20418, or may
be examined at the Center for Food Safety and Applied Nutrition's
Library, 200 C St. SW., rm. 3321, Washington, DC, or the Office of the
Federal Register, 800 North Capitol St. NW., suite 700, Washington, DC.
(c) In accordance with Sec. 184.1(b)(1), the ingredient is used in
food with no limitation other than current good manufacturing practice.
The affirmation of this ingredient as generally recognized as safe as a
direct human food ingredient is based upon the following current good
manufacturing practice conditions of use:
(1) The ingredient is used as an enzyme as defined in
Sec. 170.3(o)(9) of this chapter for the interesterification of fats
and oils.
(2) The ingredient is used in food at levels not to exceed current
good manufacturing practice.
Dated: April 14, 1998.
L. Robert Lake,
Director, Office of Policy, Planning and Strategic Initiatives, Center
for Food Safety and Applied Nutrition.
[FR Doc. 98-11681 Filed 5-1-98; 8:45 am]
BILLING CODE 4160-01-F